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Conserved domains on  [gi|1595776923|ref|NP_001356094|]
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E3 ubiquitin-protein ligase MIB2 isoform 3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
399-668 5.97e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.19  E-value: 5.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 399 EDANLDVAERARENKSSLSVALDKLRTQKSDPEHPGRLVVEAALGNVARALDLLRRHPEQVDTKN-QGRTALQVAAYLGQ 477
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDdGGNTLLHAAARNGD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 478 VELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDV 557
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 558 NLPDAHADTPLHSAISAGAGAssIVEVLTEVpGIDVTATNSQGFTLLHHASLKGHVLAVrKILARARQLVDAKKEDGFTA 637
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLE--IVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIV-KLLLEAGADLNAKDKDGLTA 255
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1595776923 638 LHLAALNNHREVAQVLIREGRCDVNVRNRKL 668
Cdd:COG0666   256 LLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
160-224 5.48e-35

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


:

Pssm-ID: 461991  Cd Length: 66  Bit Score: 127.33  E-value: 5.48e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595776923 160 GAKVVRGPDWEWGSQDGGEGKTGRVVDIRGWDVETGRSVASVTWADGTTNVYRVGHKGKVDLRCV 224
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
907-957 1.45e-28

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; 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 different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are 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 enable efficient transfer of ubiquitin from E2 to the substrates.


The actual alignment was detected with superfamily member cd16728:

Pssm-ID: 473075  Cd Length: 51  Bit Score: 108.41  E-value: 1.45e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776923 907 MEERITCPICIDSHIRLVFQCGHGACAPCGAALNACPICRQPIRDRIQIFV 957
Cdd:cd16728     1 MEERITCPICIDNHIKLVFQCGHGSCIECSSALKACPICRQAIRERIQIFV 51
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
89-133 4.95e-27

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


:

Pssm-ID: 239079  Cd Length: 45  Bit Score: 104.08  E-value: 4.95e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1595776923  89 IICDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHNKHDLTHAFERY 133
Cdd:cd02339     1 IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHDLEHRFYRY 45
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
328-392 3.51e-25

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


:

Pssm-ID: 465720  Cd Length: 67  Bit Score: 99.24  E-value: 3.51e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776923 328 FWVGDVVRVIGDLDTVKRLQAGHGEWTDDMAPALGRVGKVVKVFGDGNLRVAV--GGQRWTFSPSCL 392
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFpgGGRRWTLNPAAL 67
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
257-322 4.76e-24

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


:

Pssm-ID: 465720  Cd Length: 67  Bit Score: 96.16  E-value: 4.76e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776923 257 FQRGDKVKCLLDTDVLRDMQEGHGGWNPRMAEFIGQMGTVHRITDRGDVRVQF-NHETRWTFHPGAL 322
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFpGGGRRWTLNPAAL 67
RING-HC_MIB2_rpt1 cd16726
first RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also ...
832-869 9.72e-20

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: 82.88  E-value: 9.72e-20
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1595776923 832 AECLVCSELALLILFSPCQHRTVCEECARRMKKCIRCQ 869
Cdd:cd16726     1 SECLVCSELAALVRFEPCQHSIVCEECARRMKKCIKCQ 38
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
12-78 6.22e-18

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


:

Pssm-ID: 461991  Cd Length: 66  Bit Score: 78.80  E-value: 6.22e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776923  12 GMRVVRGMDWKWGQQDGGEGGVGTVVELGRHGSpSTPDRTVVVQWDQGTRTNYRAGYQGAHDLLLYD 78
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDS-ESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66
Ank_2 pfam12796
Ankyrin repeats (3 copies);
638-714 1.11e-11

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 1.11e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776923 638 LHLAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDaGCSVNtEDEEGDTALHVALQRHQL 714
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHL 74
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
399-668 5.97e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.19  E-value: 5.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 399 EDANLDVAERARENKSSLSVALDKLRTQKSDPEHPGRLVVEAALGNVARALDLLRRHPEQVDTKN-QGRTALQVAAYLGQ 477
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDdGGNTLLHAAARNGD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 478 VELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDV 557
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 558 NLPDAHADTPLHSAISAGAGAssIVEVLTEVpGIDVTATNSQGFTLLHHASLKGHVLAVrKILARARQLVDAKKEDGFTA 637
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLE--IVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIV-KLLLEAGADLNAKDKDGLTA 255
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1595776923 638 LHLAALNNHREVAQVLIREGRCDVNVRNRKL 668
Cdd:COG0666   256 LLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
160-224 5.48e-35

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


Pssm-ID: 461991  Cd Length: 66  Bit Score: 127.33  E-value: 5.48e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595776923 160 GAKVVRGPDWEWGSQDGGEGKTGRVVDIRGWDVETGRSVASVTWADGTTNVYRVGHKGKVDLRCV 224
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
RING-HC_MIB2_rpt2 cd16728
second RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also ...
907-957 1.45e-28

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: 108.41  E-value: 1.45e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776923 907 MEERITCPICIDSHIRLVFQCGHGACAPCGAALNACPICRQPIRDRIQIFV 957
Cdd:cd16728     1 MEERITCPICIDNHIKLVFQCGHGSCIECSSALKACPICRQAIRERIQIFV 51
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
89-133 4.95e-27

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


Pssm-ID: 239079  Cd Length: 45  Bit Score: 104.08  E-value: 4.95e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1595776923  89 IICDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHNKHDLTHAFERY 133
Cdd:cd02339     1 IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHDLEHRFYRY 45
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
328-392 3.51e-25

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


Pssm-ID: 465720  Cd Length: 67  Bit Score: 99.24  E-value: 3.51e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776923 328 FWVGDVVRVIGDLDTVKRLQAGHGEWTDDMAPALGRVGKVVKVFGDGNLRVAV--GGQRWTFSPSCL 392
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFpgGGRRWTLNPAAL 67
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
257-322 4.76e-24

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


Pssm-ID: 465720  Cd Length: 67  Bit Score: 96.16  E-value: 4.76e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776923 257 FQRGDKVKCLLDTDVLRDMQEGHGGWNPRMAEFIGQMGTVHRITDRGDVRVQF-NHETRWTFHPGAL 322
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFpGGGRRWTLNPAAL 67
PHA03095 PHA03095
ankyrin-like protein; Provisional
461-712 4.58e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 103.95  E-value: 4.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 461 TKNQGRTALQVaaYLGQ-----VELVRLLLQARASMDLPDDEGNTVLHYTAM-GNQPEATRVLLSAGCAVDARNGTRSTA 534
Cdd:PHA03095   43 RGEYGKTPLHL--YLHYssekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGRTP 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 535 LHVAVqRGF---LEVVKILCERGCDVNLPDAHADTPLHSAISAGAGASSIVEVLTEVpGIDVTATNSQGFTLLHHaslkg 611
Cdd:PHA03095  121 LHVYL-SGFninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDA-GADVYAVDDRFRSLLHH----- 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 612 HVLAVR------KILARARQLVDAKKEDGFTALHLAALNN--HREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGL 683
Cdd:PHA03095  194 HLQSFKprarivRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAG-ISINARNRYGQTPLHYAAVFNNPRA 272
                         250       260
                  ....*....|....*....|....*....
gi 1595776923 684 VPLLVDAGCSVNTEDEEGDTALHVALQRH 712
Cdd:PHA03095  273 CRRLIALGADINAVSSDGNTPLSLMVRNN 301
Ank_2 pfam12796
Ankyrin repeats (3 copies);
469-561 2.00e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 2.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 469 LQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTrsTALHVAVQRGFLEVVK 548
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1595776923 549 ILCERGCDVNLPD 561
Cdd:pfam12796  79 LLLEKGADINVKD 91
RING-HC_MIB2_rpt1 cd16726
first RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also ...
832-869 9.72e-20

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: 82.88  E-value: 9.72e-20
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1595776923 832 AECLVCSELALLILFSPCQHRTVCEECARRMKKCIRCQ 869
Cdd:cd16726     1 SECLVCSELAALVRFEPCQHSIVCEECARRMKKCIKCQ 38
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
12-78 6.22e-18

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


Pssm-ID: 461991  Cd Length: 66  Bit Score: 78.80  E-value: 6.22e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776923  12 GMRVVRGMDWKWGQQDGGEGGVGTVVELGRHGSpSTPDRTVVVQWDQGTRTNYRAGYQGAHDLLLYD 78
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDS-ESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66
Ank_2 pfam12796
Ankyrin repeats (3 copies);
638-714 1.11e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 1.11e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776923 638 LHLAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDaGCSVNtEDEEGDTALHVALQRHQL 714
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHL 74
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
564-797 2.05e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 64.65  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 564 ADTPLHSAISAGAGASsiVEVLTEVPGIDVTATNSQGFTLLHHASLKGHVLAVRKILARARQLVD----AKKEDGFTALH 639
Cdd:cd22192    17 SESPLLLAAKENDVQA--IKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 640 LAALNNHREVAQVLIREGrCDVN---------VRNRKL-----QSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTAL 705
Cdd:cd22192    95 IAVVNQNLNLVRELIARG-ADVVspratgtffRPGPKNliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 706 HV-ALQRHQLLP------LVADRAGGDPGPLQLLSrlqasglpgcteltvgaavacflalegadvsyaNHRGRSPLDLAT 778
Cdd:cd22192   174 HIlVLQPNKTFAcqmydlILSYDKEDDLQPLDLVP---------------------------------NNQGLTPFKLAA 220
                         250
                  ....*....|....*....
gi 1595776923 779 EGRVLKALQGCAQRFRERQ 797
Cdd:cd22192   221 KEGNIVMFQHLVQKRRHIQ 239
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
85-129 1.51e-08

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


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 51.29  E-value: 1.51e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1595776923   85 RHPNIICDCCKKHgLRGMRWKCRVCFDYDLCTQCYMHNKHDLTHA 129
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
86-124 1.61e-06

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


Pssm-ID: 395451  Cd Length: 45  Bit Score: 45.55  E-value: 1.61e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1595776923  86 HPNIICDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHNKH 124
Cdd:pfam00569   2 HKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKG 40
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
456-605 2.60e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 51.24  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 456 PEQVDTKNQ-GRTALQVAAYLGQV-ELVRLLLqaraSMDLPDDEGNTVLHYTAM---GNQPEATRVLLSAGC-------A 523
Cdd:TIGR00870  42 KLNINCPDRlGRSALFVAAIENENlELTELLL----NLSCRGAVGDTLLHAISLeyvDAVEAILLHLLAAFRksgplelA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 524 VDARNGTRS---TALHVAVQRGFLEVVKILCERGCDVN--------LPDAHADTPLHS----AISAGAGASSIVEVLTEV 588
Cdd:TIGR00870 118 NDQYTSEFTpgiTALHLAAHRQNYEIVKLLLERGASVParacgdffVKSQGVDSFYHGesplNAAACLGSPSIVALLSED 197
                         170
                  ....*....|....*..
gi 1595776923 589 PGiDVTATNSQGFTLLH 605
Cdd:TIGR00870 198 PA-DILTADSLGNTLLH 213
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
909-952 5.57e-05

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 41.59  E-value: 5.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1595776923 909 ERITCPICIDSHIRLVF-QCGHGA-CAPCGAAL----NACPICRQPIRDR 952
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLlPCGHLClCEECAERLlrkkKKCPICRQPIESV 50
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
833-874 1.07e-04

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 40.82  E-value: 1.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1595776923 833 ECLVCSELALLILFSPCQHRTVCEECARRM----KKCIRCQVVISK 874
Cdd:pfam13920   4 LCVICLDRPRNVVLLPCGHLCLCEECAERLlrkkKKCPICRQPIES 49
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
633-663 1.79e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 1.79e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1595776923  633 DGFTALHLAALNNHREVAQVLIREGRcDVNV 663
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA-DINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
639-708 1.51e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 1.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 639 HLAALNNhrEVAQVLIREGRCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVA 708
Cdd:PTZ00322   88 QLAASGD--AVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
399-668 5.97e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.19  E-value: 5.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 399 EDANLDVAERARENKSSLSVALDKLRTQKSDPEHPGRLVVEAALGNVARALDLLRRHPEQVDTKN-QGRTALQVAAYLGQ 477
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDdGGNTLLHAAARNGD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 478 VELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDV 557
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 558 NLPDAHADTPLHSAISAGAGAssIVEVLTEVpGIDVTATNSQGFTLLHHASLKGHVLAVrKILARARQLVDAKKEDGFTA 637
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLE--IVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIV-KLLLEAGADLNAKDKDGLTA 255
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1595776923 638 LHLAALNNHREVAQVLIREGRCDVNVRNRKL 668
Cdd:COG0666   256 LLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
416-705 9.03e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 9.03e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 416 LSVALDKLRTQKSDPEHPGRLVVEAALGNVARALDLLRRHPEQVDTKNQGRTALQVAAYLGQVELVRLLLQARASMDLPD 495
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 496 DEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAisAG 575
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA--AA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 576 AGASSIVEVLTEVpGIDVTATNSQGFTLLHHASLKGHVLAVRKILAR-ARqlVDAKKEDGFTALHLAALNNHREVAQVLI 654
Cdd:COG0666   163 NGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAgAD--VNAKDNDGKTALDLAAENGNLEIVKLLL 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776923 655 REGRcDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTAL 705
Cdd:COG0666   240 EAGA-DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
448-719 9.85e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 9.85e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 448 ALDLLRRHPEQVDTKNQGRTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDAR 527
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 528 NGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAisAGAGASSIVEVLTEvPGIDVTATNSQGFTLLHHA 607
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA--AYNGNLEIVKLLLE-AGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 608 SLKGHVLAVRKILAR-ARqlVDAKKEDGFTALHLAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVPL 686
Cdd:COG0666   161 AANGNLEIVKLLLEAgAD--VNARDNDGETPLHLAAENGHLEIVKLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIVKL 237
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1595776923 687 LVDAGCSVNTEDEEGDTALHVALQRHQLLPLVA 719
Cdd:COG0666   238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
478-713 4.54e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.24  E-value: 4.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 478 VELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDV 557
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 558 NLPDAHADTPLHSAISAGAGAssIVEVLTEvPGIDVTATNSQGFTLLHHASLKGHVLAVRKILAR-ARqlVDAKKEDGFT 636
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLE--IVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgAD--VNAQDNDGNT 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776923 637 ALHLAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVALQRHQ 713
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGN 231
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
160-224 5.48e-35

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


Pssm-ID: 461991  Cd Length: 66  Bit Score: 127.33  E-value: 5.48e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595776923 160 GAKVVRGPDWEWGSQDGGEGKTGRVVDIRGWDVETGRSVASVTWADGTTNVYRVGHKGKVDLRCV 224
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDSESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVV 65
RING-HC_MIB2_rpt2 cd16728
second RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also ...
907-957 1.45e-28

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: 108.41  E-value: 1.45e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776923 907 MEERITCPICIDSHIRLVFQCGHGACAPCGAALNACPICRQPIRDRIQIFV 957
Cdd:cd16728     1 MEERITCPICIDNHIKLVFQCGHGSCIECSSALKACPICRQAIRERIQIFV 51
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
89-133 4.95e-27

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


Pssm-ID: 239079  Cd Length: 45  Bit Score: 104.08  E-value: 4.95e-27
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1595776923  89 IICDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHNKHDLTHAFERY 133
Cdd:cd02339     1 IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGDKHDLEHRFYRY 45
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
328-392 3.51e-25

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


Pssm-ID: 465720  Cd Length: 67  Bit Score: 99.24  E-value: 3.51e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776923 328 FWVGDVVRVIGDLDTVKRLQAGHGEWTDDMAPALGRVGKVVKVFGDGNLRVAV--GGQRWTFSPSCL 392
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFpgGGRRWTLNPAAL 67
SH3_15 pfam18346
Mind bomb SH3 repeat domain; The REP domain of Mind bomb which serves as the substrate ...
257-322 4.76e-24

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


Pssm-ID: 465720  Cd Length: 67  Bit Score: 96.16  E-value: 4.76e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776923 257 FQRGDKVKCLLDTDVLRDMQEGHGGWNPRMAEFIGQMGTVHRITDRGDVRVQF-NHETRWTFHPGAL 322
Cdd:pfam18346   1 FEVGDWVRVKDDLEKVKPLQEGHGGWNGGMAETLGSVGTVVKVDADGDLRVQFpGGGRRWTLNPAAL 67
PHA03095 PHA03095
ankyrin-like protein; Provisional
461-712 4.58e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 103.95  E-value: 4.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 461 TKNQGRTALQVaaYLGQ-----VELVRLLLQARASMDLPDDEGNTVLHYTAM-GNQPEATRVLLSAGCAVDARNGTRSTA 534
Cdd:PHA03095   43 RGEYGKTPLHL--YLHYssekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGRTP 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 535 LHVAVqRGF---LEVVKILCERGCDVNLPDAHADTPLHSAISAGAGASSIVEVLTEVpGIDVTATNSQGFTLLHHaslkg 611
Cdd:PHA03095  121 LHVYL-SGFninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDA-GADVYAVDDRFRSLLHH----- 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 612 HVLAVR------KILARARQLVDAKKEDGFTALHLAALNN--HREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGL 683
Cdd:PHA03095  194 HLQSFKprarivRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAG-ISINARNRYGQTPLHYAAVFNNPRA 272
                         250       260
                  ....*....|....*....|....*....
gi 1595776923 684 VPLLVDAGCSVNTEDEEGDTALHVALQRH 712
Cdd:PHA03095  273 CRRLIALGADINAVSSDGNTPLSLMVRNN 301
Ank_2 pfam12796
Ankyrin repeats (3 copies);
469-561 2.00e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 2.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 469 LQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTrsTALHVAVQRGFLEVVK 548
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1595776923 549 ILCERGCDVNLPD 561
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
544-778 8.55e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.55  E-value: 8.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 544 LEVVKILCERGCDVNLPDAHADTPLHSAISAGAGASS-IVEVLTEVpGIDVTATNSQGFTLLHHASLKGHVLAVRKILAR 622
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdIVRLLLEA-GADVNAPERCGFTPLHLYLYNATTLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 623 ARQLVDAKKEDGFTALH--LAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQ--QAHLGLVPLLVDAGCSVNTED 698
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKG-ADVNALDLYGMTPLAVLLKsrNANVELLRLLIDAGADVYAVD 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 699 EEGDTALHVALQR--------HQLLPLVADRAGGDPGPLQLLSRLQASGlpGCTELTVGaavacFLALEGADVSYANHRG 770
Cdd:PHA03095  185 DRFRSLLHHHLQSfkprarivRELIRAGCDPAATDMLGNTPLHSMATGS--SCKRSLVL-----PLLIAGISINARNRYG 257

                  ....*...
gi 1595776923 771 RSPLDLAT 778
Cdd:PHA03095  258 QTPLHYAA 265
RING-HC_MIB2_rpt1 cd16726
first RING finger, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also ...
832-869 9.72e-20

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: 82.88  E-value: 9.72e-20
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1595776923 832 AECLVCSELALLILFSPCQHRTVCEECARRMKKCIRCQ 869
Cdd:cd16726     1 SECLVCSELAALVRFEPCQHSIVCEECARRMKKCIKCQ 38
PHA03095 PHA03095
ankyrin-like protein; Provisional
478-708 2.52e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.40  E-value: 2.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 478 VELVRLLLQARASMDLPDDEGNTVLHY---TAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGF-LEVVKILCER 553
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 554 GCDVNLPDAHADTPLHSAISAGAGASSIVEVLTEVpGIDVTATNSQGFTLLhHASLKGH--VLAVRKILARARQLVDAKK 631
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYLSGFNINPKVIRLLLRK-GADVNALDLYGMTPL-AVLLKSRnaNVELLRLLIDAGADVYAVD 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 632 EDGFTALHLAAlNNHREVAQV---LIREGrCDVNVRNRKLQSPLHLAVQQ---AHLGLVPLLvDAGCSVNTEDEEGDTAL 705
Cdd:PHA03095  185 DRFRSLLHHHL-QSFKPRARIvreLIRAG-CDPAATDMLGNTPLHSMATGsscKRSLVLPLL-IAGISINARNRYGQTPL 261

                  ...
gi 1595776923 706 HVA 708
Cdd:PHA03095  262 HYA 264
MIB_HERC2 pfam06701
Mib_herc2; Named "mib/herc2 domain" in. Usually the protein also contains an E3 ligase domain ...
12-78 6.22e-18

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


Pssm-ID: 461991  Cd Length: 66  Bit Score: 78.80  E-value: 6.22e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776923  12 GMRVVRGMDWKWGQQDGGEGGVGTVVELGRHGSpSTPDRTVVVQWDQGTRTNYRAGYQGAHDLLLYD 78
Cdd:pfam06701   1 GARVVRGPDWKWGDQDGGEGHVGTVVEIRDWDS-ESPRSTVRVQWDNGSTNVYRVGYEGKYDLKVVD 66
PHA03100 PHA03100
ankyrin repeat protein; Provisional
490-699 9.42e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.03  E-value: 9.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 490 SMDLPDDEGNTVLHYTAM-GNQPEATRVLLSAGCAVDARNGTRSTALH-----VAVQRGFLEVVKILCERGCDVNLPDAH 563
Cdd:PHA03100   26 DLNDYSYKKPVLPLYLAKeARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 564 ADTPLHSAISAGAGASSIVEVLTEVpGIDVTATNSQGFTLLHhASLKG----------------HVLAVRKI--LARARQ 625
Cdd:PHA03100  106 GITPLLYAISKKSNSYSIVEYLLDN-GANVNIKNSDGENLLH-LYLESnkidlkilkllidkgvDINAKNRVnyLLSYGV 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595776923 626 LVDAKKEDGFTALHLAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDE 699
Cdd:PHA03100  184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG-ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02876 PHA02876
ankyrin repeat protein; Provisional
478-715 3.47e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 86.66  E-value: 3.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 478 VELVRLLLQARASMDLPDDEGNTVLHYTAmgNQPEATRV---LLSAGCAVDARNGTRSTALHVAVQRGF-LEVVKILCER 553
Cdd:PHA02876  253 LETSLLLYDAGFSVNSIDDCKNTPLHHAS--QAPSLSRLvpkLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIML 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 554 GCDVNLPDAHADTPLHSAISAGAGASSIVEVLTEvpGIDVTATNSQGFTLLHHASLKGHVLAVRKILARARQLVDAKKED 633
Cdd:PHA02876  331 GADVNAADRLYITPLHQASTLDRNKDIVITLLEL--GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKI 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 634 GfTALHLAAL-NNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQ-AHLGLVPLLVDAGCSVNTEDEEGDTALHVALQR 711
Cdd:PHA02876  409 G-TALHFALCgTNPYMSVKTLIDRG-ANVNSKNKDLSTPLHYACKKnCKLDVIEMLLDNGADVNAINIQNQYPLLIALEY 486

                  ....
gi 1595776923 712 HQLL 715
Cdd:PHA02876  487 HGIV 490
Ank_2 pfam12796
Ankyrin repeats (3 copies);
604-698 3.72e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 3.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 604 LHHASLKGHVLAVrKILARARQLVDAKKEDGFTALHLAALNNHREVAQVLIREGRCDVNVRNRklqSPLHLAVQQAHLGL 683
Cdd:pfam12796   1 LHLAAKNGNLELV-KLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEI 76
                          90
                  ....*....|....*
gi 1595776923 684 VPLLVDAGCSVNTED 698
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
RING-HC_MIBs-like cd16520
RING finger, HC subclass, found in mind bomb MIB1, MIB2, RGLG1, RGLG2, and similar proteins; ...
911-949 6.53e-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: 71.94  E-value: 6.53e-16
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1595776923 911 ITCPICIDSHIRLVFQCGHGACAPCGAALNACPICRQPI 949
Cdd:cd16520     1 ILCPICMERKKNVVFLCGHGTCQKCAEKLKKCPICRKPI 39
PHA02874 PHA02874
ankyrin repeat protein; Provisional
469-777 1.11e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.78  E-value: 1.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 469 LQVAAYLGQVELVRLLLQARAS-MDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVV 547
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 548 KILCERGCDVNL---PDAHADTplhsaisagagASSIVEVltevpGIDVTATNSQGFTLLHHASLKGHvLAVRKILARAR 624
Cdd:PHA02874   85 KLLIDNGVDTSIlpiPCIEKDM-----------IKTILDC-----GIDVNIKDAELKTFLHYAIKKGD-LESIKMLFEYG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 625 QLVDAKKEDGFTALHLAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTA 704
Cdd:PHA02874  148 ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595776923 705 LHVA-LQRHQLLPLVADRAGGDPGPLQLLSRLQASGLPGCTELTVGAavacfLALEGADVSYANHRGRSPLDLA 777
Cdd:PHA02874  227 LHNAiIHNRSAIELLINNASINDQDIDGSTPLHHAINPPCDIDIIDI-----LLYHKADISIKDNKGENPIDTA 295
RING-HC_MIBs cd16519
RING finger, HC subclass, found in mind bomb MIB1, MIB2, and similar proteins; MIBs are large, ...
832-869 1.21e-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: 71.36  E-value: 1.21e-15
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1595776923 832 AECLVCSELALLILFSPCQHRTVCEECARRMKKCIRCQ 869
Cdd:cd16519     1 EECRVCSDKKALVLFQPCGHVVACEECSLRMKKCLQCK 38
Ank_2 pfam12796
Ankyrin repeats (3 copies);
502-597 1.37e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 502 LHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERgCDVNLPDaHADTPLHSAISagAGASSI 581
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAAR--SGHLEI 76
                          90
                  ....*....|....*.
gi 1595776923 582 VEVLTEvPGIDVTATN 597
Cdd:pfam12796  77 VKLLLE-KGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
521-708 2.69e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.32  E-value: 2.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 521 GCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAISAGAGASS---IVEVLTEVpGIDVTATN 597
Cdd:PHA03100   25 DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDvkeIVKLLLEY-GANVNAPD 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 598 SQGFTLLHHASLK--GHVLAVRKILARARQlVDAKKEDGFTALHLAALNNHR--EVAQVLIREG---------------R 658
Cdd:PHA03100  104 NNGITPLLYAISKksNSYSIVEYLLDNGAN-VNIKNSDGENLLHLYLESNKIdlKILKLLIDKGvdinaknrvnyllsyG 182
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1595776923 659 CDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVA 708
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
535-665 8.31e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 8.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 535 LHVAVQRGFLEVVKILCERGCDVNLpdahadtplhsaisagagassivevltevpgidvtaTNSQGFTLLHHASLKGHVL 614
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANL------------------------------------QDKNGRTALHLAAKNGHLE 44
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776923 615 AVRKILARARQLVdakKEDGFTALHLAALNNHREVAQVLIREGrCDVNVRN 665
Cdd:pfam12796  45 IVKLLLEHADVNL---KDNGRTALHYAARSGHLEIVKLLLEKG-ADINVKD 91
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
89-133 4.66e-14

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


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 67.07  E-value: 4.66e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1595776923  89 IICDCCKKHgLRGMRWKCRVCFDYDLCTQCY--MHNKHDLTHAFERY 133
Cdd:cd02249     1 YSCDGCLKP-IVGVRYHCLVCEDFDLCSSCYakGKKGHPPDHSFTEI 46
PHA02876 PHA02876
ankyrin repeat protein; Provisional
466-712 5.93e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.26  E-value: 5.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 466 RTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYT----------------------------AMGNQPEATRVL 517
Cdd:PHA02876  179 ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAvdsknidtikaiidnrsninkndlsllkAIRNEDLETSLL 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 518 L-SAGCAVDARNGTRSTALHVAVQRGFL-EVVKILCERGCDVNLPDAHADTPLHSAISAGAGASSIVEVLTEvpGIDVTA 595
Cdd:PHA02876  259 LyDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIML--GADVNA 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 596 TNSQGFTLLHHASL----KGHVLAVRKILARarqlVDAKKEDGFTALHLAALNNHREVAQVLIREGrCDVNVRNRKLQSP 671
Cdd:PHA02876  337 ADRLYITPLHQASTldrnKDIVITLLELGAN----VNARDYCDKTPIHYAAVRNNVVIINTLLDYG-ADIEALSQKIGTA 411
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1595776923 672 LHLAVQQAHLGL-VPLLVDAGCSVNTEDEEGDTALHVALQRH 712
Cdd:PHA02876  412 LHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKN 453
PHA02874 PHA02874
ankyrin repeat protein; Provisional
479-677 1.98e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.46  E-value: 1.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 479 ELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVN 558
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 559 LPDAHADTPLHSAISAGAGAsSIVEVLTEVPGIDVTATNsqGFTLLHHASLkgHVLAVRKILARARQLVDaKKEDGFTAL 638
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYA-CIKLLIDHGNHIMNKCKN--GFTPLHNAII--HNRSAIELLINNASIND-QDIDGSTPL 258
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1595776923 639 HlAALNN--HREVAQVLIREgRCDVNVRNRKLQSPLHLAVQ 677
Cdd:PHA02874  259 H-HAINPpcDIDIIDILLYH-KADISIKDNKGENPIDTAFK 297
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
483-694 1.31e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.82  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 483 LLLQARASMDLPDDEGNtVLHYTAMGNQPEATRvLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDA 562
Cdd:PLN03192  512 LLGDNGGEHDDPNMASN-LLTVASTGNAALLEE-LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDA 589
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 563 HADTPLHSAISagAGASSIVEVLTEVpgidVTATNSQ-GFTLLHHASLKGHVLAVRKILARARQlVDAKKEDGFTALHLA 641
Cdd:PLN03192  590 NGNTALWNAIS--AKHHKIFRILYHF----ASISDPHaAGDLLCTAAKRNDLTAMKELLKQGLN-VDSEDHQGATALQVA 662
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1595776923 642 ALNNHREVAQVLIREGRCDVNVRNRKLQSPLHL--AVQQAHLGLVPLLVDAGCSV 694
Cdd:PLN03192  663 MAEDHVDMVRLLIMNGADVDKANTDDDFSPTELreLLQKRELGHSITIVDSVPAD 717
PHA02874 PHA02874
ankyrin repeat protein; Provisional
458-607 1.52e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.76  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 458 QVDTKN-QGRTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALH 536
Cdd:PHA02874  116 DVNIKDaELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595776923 537 VAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAISAGagaSSIVEVLTEVPGIDVTATNsqGFTLLHHA 607
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN---RSAIELLINNASINDQDID--GSTPLHHA 261
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
581-786 4.79e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.67  E-value: 4.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 581 IVEVLTEVPGIDVTATNSQGFTLLHHASLKGHVLAVRKILARARQLVDAKKEDGFTALHLAALNNHREVAQVLIREGRcD 660
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-D 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 661 VNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVALQRHQLlplvadraggdpgplqllsrlqasgl 740
Cdd:COG0666    80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL-------------------------- 133
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1595776923 741 pgcteltvgAAVACFLALeGADVSYANHRGRSPLDLATEGR---VLKAL 786
Cdd:COG0666   134 ---------EIVKLLLEA-GADVNAQDNDGNTPLHLAAANGnleIVKLL 172
PHA02876 PHA02876
ankyrin repeat protein; Provisional
477-709 7.57e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.32  E-value: 7.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 477 QVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAG---------------CAVDARN--------GTRST 533
Cdd:PHA02876  157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGadvniialddlsvleCAVDSKNidtikaiiDNRSN 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 534 ------ALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAISAGAgASSIVEVLTEvPGIDVTATNSQGFTLLHHA 607
Cdd:PHA02876  237 inkndlSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPS-LSRLVPKLLE-RGADVNAKNIKGETPLYLM 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 608 SLKGH-VLAVRKILARARQlVDAKKEDGFTALHLAA-LNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVP 685
Cdd:PHA02876  315 AKNGYdTENIRTLIMLGAD-VNAADRLYITPLHQAStLDRNKDIVITLLELG-ANVNARDYCDKTPIHYAAVRNNVVIIN 392
                         250       260
                  ....*....|....*....|....
gi 1595776923 686 LLVDAGCSVNTEDEEGDTALHVAL 709
Cdd:PHA02876  393 TLLDYGADIEALSQKIGTALHFAL 416
PHA02878 PHA02878
ankyrin repeat protein; Provisional
477-678 1.10e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.37  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 477 QVELVRLLLQARASMDLPD-DEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGC 555
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 556 DVNLPDAHADTPLHsaISAGAGAS-SIVEVLTEvPGIDVTATNSqgftllhhaslkghvlavrkILararqlvdakkedG 634
Cdd:PHA02878  226 STDARDKCGNTPLH--ISVGYCKDyDILKLLLE-HGVDVNAKSY--------------------IL-------------G 269
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1595776923 635 FTALHLAAlnnHREVAQVLIREGRCDVNVRNRKLQSPLHLAVQQ 678
Cdd:PHA02878  270 LTALHSSI---KSERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank_2 pfam12796
Ankyrin repeats (3 copies);
638-714 1.11e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 1.11e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776923 638 LHLAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDaGCSVNtEDEEGDTALHVALQRHQL 714
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHL 74
PHA03095 PHA03095
ankyrin-like protein; Provisional
444-653 2.32e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.36  E-value: 2.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 444 NVARALdlLRRHPEQVDTKNQGRTALqvAAYLGQ----VELVRLLLQARASMDLPDDEGNTVLHYTAMgnqpeatrvlls 519
Cdd:PHA03095  133 KVIRLL--LRKGADVNALDLYGMTPL--AVLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQ------------ 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 520 agcAVDARNGtrstalhvavqrgfleVVKILCERGCDVNLPDAHADTPLHSAISAGAGASSIVEVLTEvPGIDVTATNSQ 599
Cdd:PHA03095  197 ---SFKPRAR----------------IVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPLLI-AGISINARNRY 256
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1595776923 600 GFTLLHHASLKGHVLAVRKILARARQlVDAKKEDGFTALHLAALN-NHREVAQVL 653
Cdd:PHA03095  257 GQTPLHYAAVFNNPRACRRLIALGAD-INAVSSDGNTPLSLMVRNnNGRAVRAAL 310
RING-HC_RGLG_plant cd16729
RING finger, HC subclass, found in RING domain ligase RGLG1, RGLG2 and similar proteins from ...
913-956 3.20e-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: 59.03  E-value: 3.20e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1595776923 913 CPICIDSHIRLVFQCGHGACAPCGAALNACPICRQPIRDRIQIF 956
Cdd:cd16729     5 CPICLSNPKDMAFGCGHQTCCECGQSLTHCPICRQPITTRIKLY 48
PHA02878 PHA02878
ankyrin repeat protein; Provisional
461-652 4.50e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 4.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 461 TKNQGRTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQ 540
Cdd:PHA02878  164 DRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVG 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 541 RGF-LEVVKILCERGCDVNLPDAHAD-TPLHSAISagagASSIVEVLTEVpGIDVTATNSQGFTLLHHASLKGHVLAVRK 618
Cdd:PHA02878  244 YCKdYDILKLLLEHGVDVNAKSYILGlTALHSSIK----SERKLKLLLEY-GADINSLNSYKLTPLSSAVKQYLCINIGR 318
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1595776923 619 ILA-----RARQLVDAKKEDGFTaLHLAALNNHREVAQV 652
Cdd:PHA02878  319 ILIsniclLKRIKPDIKNSEGFI-DNMDCITSNKRLNQI 356
RING-HC_MIB1_rpt3 cd16727
third RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
913-956 1.00e-10

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: 57.45  E-value: 1.00e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1595776923 913 CPICIDSHIRLVFQCGHGACAPCGAALNACPICRQPIRDRIQIF 956
Cdd:cd16727     3 CPVCLDRLKNMIFLCGHGTCQLCGDRMSECPICRKAIEKRILLY 46
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
564-797 2.05e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 64.65  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 564 ADTPLHSAISAGAGASsiVEVLTEVPGIDVTATNSQGFTLLHHASLKGHVLAVRKILARARQLVD----AKKEDGFTALH 639
Cdd:cd22192    17 SESPLLLAAKENDVQA--IKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNepmtSDLYQGETALH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 640 LAALNNHREVAQVLIREGrCDVN---------VRNRKL-----QSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTAL 705
Cdd:cd22192    95 IAVVNQNLNLVRELIARG-ADVVspratgtffRPGPKNliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 706 HV-ALQRHQLLP------LVADRAGGDPGPLQLLSrlqasglpgcteltvgaavacflalegadvsyaNHRGRSPLDLAT 778
Cdd:cd22192   174 HIlVLQPNKTFAcqmydlILSYDKEDDLQPLDLVP---------------------------------NNQGLTPFKLAA 220
                         250
                  ....*....|....*....
gi 1595776923 779 EGRVLKALQGCAQRFRERQ 797
Cdd:cd22192   221 KEGNIVMFQHLVQKRRHIQ 239
PHA03100 PHA03100
ankyrin repeat protein; Provisional
442-588 2.60e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.53  E-value: 2.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 442 LGNVARALDLLRRHPEQVDTK-NQGRTALQVAAY--LGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPE------ 512
Cdd:PHA03100   82 LTDVKEIVKLLLEYGANVNAPdNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkilkl 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 513 ----------ATRV--LLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAIsagagASS 580
Cdd:PHA03100  162 lidkgvdinaKNRVnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI-----LNN 236

                  ....*...
gi 1595776923 581 IVEVLTEV 588
Cdd:PHA03100  237 NKEIFKLL 244
PHA02878 PHA02878
ankyrin repeat protein; Provisional
535-711 5.45e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 5.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 535 LHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAISAgAGASSIVEVLTEVPGIDVTAT-----------NSQGFTL 603
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKE-PNKLGMKEMIRSINKCSVFYTlvaikdafnnrNVEIFKI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 604 LHHASLKG------------------HVLAVRKILARARQLVDAKKEDGFTALHLAALNNHREVAQVLIREGrCDVNVRN 665
Cdd:PHA02878  120 ILTNRYKNiqtidlvyidkkskddiiEAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYG-ANVNIPD 198
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1595776923 666 RKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVALQR 711
Cdd:PHA02878  199 KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY 244
RING-HC_BIRC4_8 cd16714
RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP ...
905-956 5.52e-10

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: 55.92  E-value: 5.52e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1595776923 905 RQMEERITCPICIDSHIRLVF-QCGH-GACAPCGAALNACPICRQPIRDRIQIF 956
Cdd:cd16714     9 RRLQEEKLCKICMDRNISIVFiPCGHlVTCKQCAEALDKCPICCTVITFKQKIF 62
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
89-130 7.66e-10

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


Pssm-ID: 239080  Cd Length: 43  Bit Score: 54.96  E-value: 7.66e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1595776923  89 IICDCCKKHgLRGMRWKCRVCFDYDLCTQCYMHNKHDlTHAF 130
Cdd:cd02340     1 VICDGCQGP-IVGVRYKCLVCPDYDLCESCEAKGVHP-EHAM 40
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
429-600 4.27e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 4.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 429 DPEHPGRLVVEAALGNVARALDLLR--RHPEQVDTKnqGRTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVL---- 502
Cdd:PLN03192  522 DPNMASNLLTVASTGNAALLEELLKakLDPDIGDSK--GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnai 599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 503 ---HYT------------------------AMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGC 555
Cdd:PLN03192  600 sakHHKifrilyhfasisdphaagdllctaAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1595776923 556 DV---NLPDAHADTPLHSAISAGAGASSIVEVLTeVPGIDVTATNSQG 600
Cdd:PLN03192  680 DVdkaNTDDDFSPTELRELLQKRELGHSITIVDS-VPADEPDLGRDGG 726
Ank_5 pfam13857
Ankyrin repeats (many copies);
653-708 5.03e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.12  E-value: 5.03e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1595776923 653 LIREGRCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVA 708
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
604-709 6.81e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.23  E-value: 6.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 604 LHHASLKGHVLAVRKILARARQLVDAKKEDGFTALHLAALNNHREVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGL 683
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARG-ADPDIPNTDKFSPLHLAVMMGDIKG 150
                          90       100
                  ....*....|....*....|....*.
gi 1595776923 684 VPLLVDAGCSVNTEDEEGDTALHVAL 709
Cdd:PHA02875  151 IELLIDHKACLDIEDCCGCTPLIIAM 176
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
85-129 1.51e-08

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


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 51.29  E-value: 1.51e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1595776923   85 RHPNIICDCCKKHgLRGMRWKCRVCFDYDLCTQCYMHNKHDLTHA 129
Cdd:smart00291   1 VHHSYSCDTCGKP-IVGVRYHCLVCPDYDLCQSCFAKGSAGGEHS 44
RING-HC_BIRC2_3_7 cd16713
RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar ...
905-957 1.58e-08

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: 51.70  E-value: 1.58e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1595776923 905 RQMEERITCPICIDSHIRLVF-QCGH-GACAPCGAALNACPICRQPIRDRIQIFV 957
Cdd:cd16713     2 RRLQEERTCKVCMDKEVSIVFiPCGHlVVCTECAPSLRKCPICRATIKGTVRTFL 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
465-518 1.67e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 1.67e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1595776923 465 GRTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLL 518
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
539-707 1.70e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.54  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 539 VQRGFLEVVKILCERGCDVNLPDAHADTPLHSAisAGAGASSIVEVLTEVpGIDVTATNSQGFTLLHHASLKGHVLAVRK 618
Cdd:PHA02876  153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYA--AERGNAKMVNLLLSY-GADVNIIALDDLSVLECAVDSKNIDTIKA 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 619 ILARARQLvdaKKEDgfTALhLAALNNHREVAQVLIREGRCDVNVRNRKLQSPLHLAVQQAHLG-LVPLLVDAGCSVNTE 697
Cdd:PHA02876  230 IIDNRSNI---NKND--LSL-LKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAK 303
                         170
                  ....*....|
gi 1595776923 698 DEEGDTALHV 707
Cdd:PHA02876  304 NIKGETPLYL 313
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
428-662 5.65e-08

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 56.69  E-value: 5.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 428 SDPEHPGRLVVEAALGNVARALdllrrhpEQVDTKNQGRTALQVAAYLGQVELVRLLLQ-------ARASMDLPD----- 495
Cdd:cd22194    15 DDMDSPQSPQDDTPSNPNSPSA-------ELAKEEQRDKKKRLKKVSEAAVEELGELLKelkdlsrRRRKTDVPDflmhk 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 496 ----DEGNTVLHYTAMG---NQPEATRVLLS----AGC-------AVDARNGTRSTALHVAVQRGFLEVVKILCERGCDV 557
Cdd:cd22194    88 ltasDTGKTCLMKALLNineNTKEIVRILLAfaeeNGIldrfinaEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 558 NlpdAHA-----------------DTPLhsAISAGAGASSIVEVLTEVPGIDVTATNSQGFTLLH-----HASLKGHVLA 615
Cdd:cd22194   168 N---AHAkgvffnpkykhegfyfgETPL--ALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLHalvtvAEDSKTQNDF 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1595776923 616 VR----KILARA--RQLVDAKKEDGFTALHLAALNNHREVAQ-VLIREGRCDVN 662
Cdd:cd22194   243 VKrmydMILLKSenKNLETIRNNEGLTPLQLAAKMGKAEILKyILSREIKEKPN 296
RING-HC_MIB1_rpt2 cd16725
second RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
833-869 7.99e-08

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: 49.02  E-value: 7.99e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1595776923 833 ECLVCSELALLILFSPCQHRTVCEECARRMKKCIRCQ 869
Cdd:cd16725     2 ECVVCSDKKASVLFKPCGHMCACEGCAALMKKCVQCR 38
Ank_5 pfam13857
Ankyrin repeats (many copies);
517-571 1.07e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 1.07e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1595776923 517 LLSAG-CAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSA 571
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ZZ_HERC2 cd02344
Zinc finger, ZZ type. Zinc finger present in HERC2 and related proteins. HERC2 is a potential ...
89-132 1.80e-07

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


Pssm-ID: 239084  Cd Length: 45  Bit Score: 48.35  E-value: 1.80e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1595776923  89 IICDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHNKHDLTHAFER 132
Cdd:cd02344     1 VTCDGCQMFPINGPRFKCRNCDDFDFCENCFKTRKHNTRHTFGR 44
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
89-131 1.89e-07

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


Pssm-ID: 239078  Cd Length: 49  Bit Score: 48.50  E-value: 1.89e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1595776923  89 IICDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHN----KHDLTHAFE 131
Cdd:cd02338     1 VSCDGCGKSNFTGRRYKCLICYDYDLCADCYDSGvtteRHLFDHPMQ 47
PHA02875 PHA02875
ankyrin repeat protein; Provisional
442-559 2.57e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 442 LGNVARALDLLR---RHPEQVDTKNQGRTA-LQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVL 517
Cdd:PHA02875  108 LATILKKLDIMKlliARGADPDIPNTDKFSpLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1595776923 518 LSAGCAVD--ARNGTrSTALHVAVQRGFLEVVKILCERGCDVNL 559
Cdd:PHA02875  188 LDSGANIDyfGKNGC-VAALCYAIENNKIDIVRLFIKRGADCNI 230
RING-HC_CARP cd16500
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, ...
912-956 4.68e-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: 47.38  E-value: 4.68e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1595776923 912 TCPICIDSHIRLVF-QCGH-GACAPCGAALNACPICRQPIRDRIQIF 956
Cdd:cd16500     2 LCKICMDAAIDCVLlECGHmVTCTDCGKKLSECPICRQYVVRVVHFF 48
PHA02876 PHA02876
ankyrin repeat protein; Provisional
516-715 5.15e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 5.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 516 VLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAISAGA--GASSIVEVLTEVPGIDV 593
Cdd:PHA02876  163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNidTIKAIIDNRSNINKNDL 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 594 TATNS--------------QGFTL----------LHHASLKGHV-LAVRKILARARQlVDAKKEDGFTALHLAALNNH-R 647
Cdd:PHA02876  243 SLLKAirnedletslllydAGFSVnsiddckntpLHHASQAPSLsRLVPKLLERGAD-VNAKNIKGETPLYLMAKNGYdT 321
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595776923 648 EVAQVLIREGrCDVNVRNRKLQSPLHLA-VQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVALQRHQLL 715
Cdd:PHA02876  322 ENIRTLIMLG-ADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVV 389
mRING-HC-C3HC5_NEU1 cd16647
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, ...
912-956 5.32e-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: 5.32e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776923 912 TCPICIDSHIRLVF-QCGHG-ACAPCGAAL----NACPICRQPIRDRIQIF 956
Cdd:cd16647     3 ECVICYERPVDTVLyRCGHMcMCYDCALQLkrrgGSCPICRAPIKDVIKIY 53
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
91-128 8.00e-07

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


Pssm-ID: 239074  Cd Length: 49  Bit Score: 46.58  E-value: 8.00e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1595776923  91 CDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHNKHDLTH 128
Cdd:cd02334     3 CNICKEFPITGFRYRCLKCFNYDLCQSCFFSGRTSKSH 40
PHA02875 PHA02875
ankyrin repeat protein; Provisional
448-575 9.73e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 9.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 448 ALDLLRRHPEQVDTKNQG-RTALQVAAYLGQVELVRLLLQARASM-DLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVD 525
Cdd:PHA02875   50 AIKLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPD 129
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1595776923 526 ARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAISAG 575
Cdd:PHA02875  130 IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
PHA02875 PHA02875
ankyrin repeat protein; Provisional
464-558 1.05e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 464 QGRTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGF 543
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180
                          90
                  ....*....|....*
gi 1595776923 544 LEVVKILCERGCDVN 558
Cdd:PHA02875  181 IAICKMLLDSGANID 195
RING-HC_MIB1_rpt1 cd16724
first RING finger, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also ...
833-869 1.09e-06

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: 45.94  E-value: 1.09e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1595776923 833 ECLVCSELALLILFSPCQHRTVCEECARRMKKCIRCQ 869
Cdd:cd16724     2 ECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICK 38
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
472-658 1.50e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.94  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 472 AAYLGQVELVRLLL-------QARASMdlpddeGNTVLHYTAMGNQPEATRVLLSAG-------CAVDARNGtrSTALHV 537
Cdd:cd22192    24 AAKENDVQAIKKLLkcpscdlFQRGAL------GETALHVAALYDNLEAAVVLMEAApelvnepMTSDLYQG--ETALHI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 538 AVQRGFLEVVKILCERGCDVNLPDA--------------HADTPLHSAisAGAGASSIVEVLTEvPGIDVTATNSQGFTL 603
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFA--ACVGNEEIVRLLIE-HGADIRAQDSLGNTV 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595776923 604 LHHASLKGHVLAVRK----ILARARQLVDAKKE-----DGFTALHLAALNNHREVAQVLIREGR 658
Cdd:cd22192   173 LHILVLQPNKTFACQmydlILSYDKEDDLQPLDlvpnnQGLTPFKLAAKEGNIVMFQHLVQKRR 236
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
86-124 1.61e-06

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


Pssm-ID: 395451  Cd Length: 45  Bit Score: 45.55  E-value: 1.61e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1595776923  86 HPNIICDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHNKH 124
Cdd:pfam00569   2 HKVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTHKG 40
Ank_4 pfam13637
Ankyrin repeats (many copies);
498-550 1.83e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1595776923 498 GNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKIL 550
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
RING-HC_IAPs cd16510
RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently ...
912-947 1.87e-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: 45.33  E-value: 1.87e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1595776923 912 TCPICIDSHIRLVFQ-CGH-GACAPCGAALNACPICRQ 947
Cdd:cd16510     3 LCKICMDREVNIVFLpCGHlVTCAQCAASLRKCPICRT 40
Ank_4 pfam13637
Ankyrin repeats (many copies);
602-654 2.02e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1595776923 602 TLLHHASLKGHVLAVRKILArARQLVDAKKEDGFTALHLAALNNHREVAQVLI 654
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLE-KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
456-605 2.60e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 51.24  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 456 PEQVDTKNQ-GRTALQVAAYLGQV-ELVRLLLqaraSMDLPDDEGNTVLHYTAM---GNQPEATRVLLSAGC-------A 523
Cdd:TIGR00870  42 KLNINCPDRlGRSALFVAAIENENlELTELLL----NLSCRGAVGDTLLHAISLeyvDAVEAILLHLLAAFRksgplelA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 524 VDARNGTRS---TALHVAVQRGFLEVVKILCERGCDVN--------LPDAHADTPLHS----AISAGAGASSIVEVLTEV 588
Cdd:TIGR00870 118 NDQYTSEFTpgiTALHLAAHRQNYEIVKLLLERGASVParacgdffVKSQGVDSFYHGesplNAAACLGSPSIVALLSED 197
                         170
                  ....*....|....*..
gi 1595776923 589 PGiDVTATNSQGFTLLH 605
Cdd:TIGR00870 198 PA-DILTADSLGNTLLH 213
PHA02874 PHA02874
ankyrin repeat protein; Provisional
532-710 2.74e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 532 STALHVAVQRGFLEVV-KILCERGCDVNLPDAHADTPLHSAISAGAgaSSIVEVLTEvPGIDVTATNsqgfTLLHHASLK 610
Cdd:PHA02874    2 SQDLRMCIYSGDIEAIeKIIKNKGNCINISVDETTTPLIDAIRSGD--AKIVELFIK-HGADINHIN----TKIPHPLLT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 611 GhvlavrkILARARQLVDAKKEDGF--TALHLAALNNhrEVAQVLIREGrCDVNVRNRKLQSPLHLAVQQAHLGLVPLLV 688
Cdd:PHA02874   75 A-------IKIGAHDIIKLLIDNGVdtSILPIPCIEK--DMIKTILDCG-IDVNIKDAELKTFLHYAIKKGDLESIKMLF 144
                         170       180
                  ....*....|....*....|..
gi 1595776923 689 DAGCSVNTEDEEGDTALHVALQ 710
Cdd:PHA02874  145 EYGADVNIEDDNGCYPIHIAIK 166
Ank_5 pfam13857
Ankyrin repeats (many copies);
619-675 5.56e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 5.56e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776923 619 ILARARQLVDAKKEDGFTALHLAALNNHREVAQVLIrEGRCDVNVRNRKLQSPLHLA 675
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
533-705 6.14e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 6.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 533 TALHVAVQRGFLEVVKILCERGC--DVNLPDAhaDTPLHSAISAGAGASsiVEVLTEVPGIDVTATNSQGFTLLHHASLK 610
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI--ESELHDAVEEGDVKA--VEELLDLGKFADDVFYKDGMTPLHLATIL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 611 GHVLAVRKILARARQlVDAKKEDGFTALHLAALNNHREVAQVLIREGRCdVNVRNRKLQSPLHLAVQQAHLGLVPLLVDA 690
Cdd:PHA02875  113 KKLDIMKLLIARGAD-PDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190
                         170
                  ....*....|....*
gi 1595776923 691 GCSVNTEDEEGDTAL 705
Cdd:PHA02875  191 GANIDYFGKNGCVAA 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
440-495 6.15e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.49  E-value: 6.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1595776923 440 AALGNVARALDLLRRHPeQVDTKNQGRTALQVAAYLGQVELVRLLLQARASMDLPD 495
Cdd:pfam12796  37 AAKNGHLEIVKLLLEHA-DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
515-585 7.53e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 7.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595776923 515 RVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAISAGAGasSIVEVL 585
Cdd:PTZ00322   99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR--EVVQLL 167
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
603-776 9.76e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.48  E-value: 9.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 603 LLHHASLKGhvlavrkiLARARQLVDAKKEDG-----FTALHLAALNNhREVAQVLIREGRcDVNVRNRKLQSPLHLAVQ 677
Cdd:PLN03192  498 LQHHKELHD--------LNVGDLLGDNGGEHDdpnmaSNLLTVASTGN-AALLEELLKAKL-DPDIGDSKGRTPLHIAAS 567
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 678 QAHLGLVPLLVDAGCSVNTEDEEGDTALHVALQR---------HQLLPLVADRAGGD-------PGPLQLLSRLQASGL- 740
Cdd:PLN03192  568 KGYEDCVLVLLKHACNVHIRDANGNTALWNAISAkhhkifrilYHFASISDPHAAGDllctaakRNDLTAMKELLKQGLn 647
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1595776923 741 ------PGCTELTVGAA-----VACFLALEGADVSYAN-HRGRSPLDL 776
Cdd:PLN03192  648 vdsedhQGATALQVAMAedhvdMVRLLIMNGADVDKANtDDDFSPTEL 695
mRING-HC-C3HC5_NEU1B cd16786
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1B (NEURL1B); ...
913-956 1.15e-05

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: 43.78  E-value: 1.15e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776923 913 CPICIDSHIRLV-FQCGHGA-CAPCGAAL----NAC-PICRQPIRDRIQIF 956
Cdd:cd16786     5 CTVCFDSEVDTViYTCGHMClCNSCGLKLkrqiNACcPICRRVIKDVIKIY 55
RING-HC_CblA-like cd16501
RING finger, HC subclass, found in Dictyostelium discoideum Cbl-like protein A (CblA) and ...
913-956 1.25e-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: 43.25  E-value: 1.25e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1595776923 913 CPICIDSHIRLVF-QCGHGACAP-CGAALNACPICRQPIRDRIQIF 956
Cdd:cd16501     8 CVVCMDAPIDTVFlECGHLACCRlCSKRLRVCPICRQPISRVVRIF 53
RING-HC_CARP2 cd16707
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 2 (CARP-2) ...
913-956 1.82e-05

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: 43.04  E-value: 1.82e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1595776923 913 CPICIDSHIRLVF-QCGHG-ACAPCGAALNACPICRQPIRDRIQIF 956
Cdd:cd16707     5 CKICMDSPIDCVLlECGHMvTCTKCGKRMSECPICRQYVIRAVHVF 50
RING-HC_LRSAM1 cd16515
RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing ...
913-955 2.18e-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: 42.67  E-value: 2.18e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1595776923 913 CPICIDSHIRLVF-QCGH-GACAPCGAALNACPICRQPIRDRIQI 955
Cdd:cd16515     4 CVVCMDAESQVIFlPCGHvCCCQTCSSSLSTCPLCRADITQRVRI 48
ZZ_dah cd02345
Zinc finger, ZZ type. Zinc finger present in Drosophila dah and related proteins. The ZZ motif ...
89-128 4.04e-05

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


Pssm-ID: 239085  Cd Length: 49  Bit Score: 41.81  E-value: 4.04e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1595776923  89 IICDCCKKHGLRGMRWKCRVCFDYDLCTQCYMHNKHDLTH 128
Cdd:cd02345     1 LSCSACRKQDISGIRFPCQVCRDYSLCLGCYTKGRETKRH 40
RING-HC_SIAH2 cd16752
RING finger, HC subclass, found in seven in absentia homolog 2 (SIAH2) and similar proteins; ...
913-949 4.53e-05

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: 41.90  E-value: 4.53e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1595776923 913 CPICIDSHIRLVFQC--GHGACAPCGAALNACPICRQPI 949
Cdd:cd16752     6 CPVCFDYVLPPILQCqaGHLVCNQCRQKLSCCPTCRGPL 44
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
909-952 5.57e-05

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 41.59  E-value: 5.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1595776923 909 ERITCPICIDSHIRLVF-QCGHGA-CAPCGAAL----NACPICRQPIRDR 952
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLlPCGHLClCEECAERLlrkkKKCPICRQPIESV 50
Ank_5 pfam13857
Ankyrin repeats (many copies);
451-504 5.59e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 5.59e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1595776923 451 LLRRHPEQVDTKNQ-GRTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHY 504
Cdd:pfam13857   1 LLEHGPIDLNRLDGeGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
RING-HC_LRSAM1 cd16515
RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing ...
833-877 5.72e-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: 41.51  E-value: 5.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1595776923 833 ECLVCSELALLILFSPCQHRTVCEECARRMKKCIRCQVVISKKLR 877
Cdd:cd16515     3 ECVVCMDAESQVIFLPCGHVCCCQTCSSSLSTCPLCRADITQRVR 47
RING-HC_SIAH1 cd16751
RING finger, HC subclass, found in seven in absentia homolog 1 (SIAH1) and similar proteins; ...
913-948 6.65e-05

RING finger, HC subclass, found in seven in absentia homolog 1 (SIAH1) and similar proteins; SIAH1, also known as Siah-1a, is an inducible E3 ubiquitin-protein ligase that contributes to proteasome-mediated degradation of multiple targets in numerous cellular processes including apoptosis, tumor suppression, cell cycle, axon guidance, transcription regulation, and tumor necrosis factor signaling. SIAH1 functions as a scaffolding protein and interacts with a variety of different substrates for ubiquitination and subsequent degradation. It regulates the oncoprotein p34SEI-1 polyubiquitination and its subsequent degradation in a p53-dependent manner, which mediates p53 preferential vitamin C cytotoxicity. It targets the nonreceptor tyrosine kinase activated Cdc42-associated kinase 1 (ACK1), a valid target in cancer therapy, for ubiquitinylation and proteasomal degradation. It also interacts with KLF10 and targets it for degradation. The CDK2 phosphorylation-mediated KLF10 dissociation from SIAH1 is linked to cell cycle progression. Moreover, SIAH1 is downregulated and associated with apoptosis and invasion in human breast cancer. It targets TAp73, a homolog of the tumor suppressor p53, for degradation. It is suppressed by hypoxia-inducible factor 1-alpha (HIF-1alpha) under hypoxic conditions to regulate TAp73 levels. It also promotes the migration and invasion of human glioma cells by regulating HIF-1alpha signaling under hypoxia. Furthermore, SIAH1 forms a protein complex with glyceraldehyde-3-phosphate dehydrogenase (GAPDH). The apoptosis signal-regulating kinase 1 (ASK1) functions as an activator of the GAPDH-Siah1 stress-signaling cascade. It also plays an important role in ethanol-induced apoptosis in neural crest cells (NCCs). SIAH1 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: 438409 [Multi-domain]  Cd Length: 45  Bit Score: 41.04  E-value: 6.65e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1595776923 913 CPICIDSHIRLVFQC--GHGACAPCGAALNACPICRQP 948
Cdd:cd16751     8 CPVCFDYVLPPILQCqsGHLVCSNCRPKLTCCPTCRGP 45
RING-HC_TRIM21_C-IV cd16596
RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar ...
906-948 7.92e-05

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: 41.81  E-value: 7.92e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1595776923 906 QMEERITCPICIDSHIRLV-FQCGHGACAPCGAAL-----NACPICRQP 948
Cdd:cd16596     5 MMWEEVTCPICLDPFVEPVsIECGHSFCQECISQVgkgggSVCPVCRQR 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
481-606 8.56e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 8.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 481 VRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLEVVKILCERGCDVNLP 560
Cdd:PHA03100  175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1595776923 561 DAH----ADTPLHSAISAGAGASSIVEVLTEVPGIDVTATNSQGFTLLHH 606
Cdd:PHA03100  255 IETllyfKDKDLNTITKIKMLKKSIMYMFLLDPGFYKNRKLIENSKSLKD 304
RING-HC_RNF180 cd16554
RING finger, HC subclass, found in RING finger protein 180 (RNF180) and similar proteins; ...
909-950 8.63e-05

RING finger, HC subclass, found in RING finger protein 180 (RNF180) and similar proteins; RNF180, also known as Rines, is a membrane-bound E3 ubiquitin-protein ligase well conserved among vertebrates. It is a critical regulator of the monoaminergic system, as well as emotional and social behavior. It interacts with brain monoamine oxidase A (MAO-A) and targets it for ubiquitination and degradation. It also functions as a novel tumor suppressor in gastric carcinogenesis. The hypermethylated CpG site count of the RNF180 DNA promoter can be used to predict survival of gastric cancer. RNF180 contains a novel conserved dual specificity protein phosphatase Rines conserved (DSPRC) domain, a basic coiled-coil domain, a C3HC4-type RING-HC finger, and a C-terminal hydrophobic region that is predicted to be a transmembrane domain.


Pssm-ID: 438216 [Multi-domain]  Cd Length: 59  Bit Score: 41.14  E-value: 8.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776923 909 ERITCPICIDSHIR--LVFQCGHGACAPCGAALNA-------CPICRQPIR 950
Cdd:cd16554     1 ESLTCPVCLDLYYDpyMCYPCGHIFCEPCLRQLAKsspkntpCPLCRTTIR 51
RING-HC_RNF170 cd16553
RING finger, HC subclass, found in RING finger protein 170 (RNF170) and similar proteins; ...
912-949 9.30e-05

RING finger, HC subclass, found in RING finger protein 170 (RNF170) and similar proteins; RNF170, also known as putative LAG1-interacting protein, is an endoplasmic reticulum (ER) membrane-bound E3 ubiquitin-protein ligase that mediates ubiquitination-dependent degradation of type-I inositol 1,4,5-trisphosphate (IP3) receptors (ITPR1) via the endoplasmic-reticulum-associated protein degradation (ERAD) pathway. A point mutation (arginine to cysteine at position 199) in the RNF170 gene is linked with autosomal-dominant sensory ataxia (ADSA), a disease characterized by neurodegeneration in the posterior columns of the spinal cord. RNF170 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438215 [Multi-domain]  Cd Length: 57  Bit Score: 41.12  E-value: 9.30e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1595776923 912 TCPICIDSHIRLV-FQCGHGACAPC-------GAALNA--CPICRQPI 949
Cdd:cd16553     3 ECPICLQDARFPVeTNCGHLFCGPCiitywrhGSWLGAvsCPVCRQTV 50
RING-HC_UNKL cd16772
RING finger, HC subclass, found in RING finger protein unkempt-like (UNKL) and similar ...
833-874 9.55e-05

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: 40.54  E-value: 9.55e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1595776923 833 ECLVCSELALLILFSPCQHRTVCEECARRMKKCIRCQVVISK 874
Cdd:cd16772     2 KCIVCQERDRSIVLQPCQHYVLCEHCAASKPECPYCKTKILK 43
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
574-662 1.05e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 574 AGAGASSIVEVLTEvPGIDVTATNSQGFTLLHHASLKGHVLAVRKILARARQlVDAKKEDGFTALHLAALNNHREVAQVL 653
Cdd:PTZ00322   90 AASGDAVGARILLT-GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD-PTLLDKDGKTPLELAEENGFREVVQLL 167

                  ....*....
gi 1595776923 654 IREGRCDVN 662
Cdd:PTZ00322  168 SRHSQCHFE 176
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
833-874 1.07e-04

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 40.82  E-value: 1.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1595776923 833 ECLVCSELALLILFSPCQHRTVCEECARRM----KKCIRCQVVISK 874
Cdd:pfam13920   4 LCVICLDRPRNVVLLPCGHLCLCEECAERLlrkkKKCPICRQPIES 49
mRING-HC-C3HC5_NEU1A cd16785
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1A (NEURL1A) ...
913-956 1.08e-04

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: 41.12  E-value: 1.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776923 913 CPICIDSHI-RLVFQCGHGA-CAPCG----AALNA-CPICRQPIRDRIQIF 956
Cdd:cd16785     7 CTICYENAVdTVIYTCGHMClCYACGlrlkKMLNAcCPICRRAIKDIIKTY 57
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
91-125 1.20e-04

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


Pssm-ID: 239077  Cd Length: 41  Bit Score: 40.24  E-value: 1.20e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1595776923  91 CDCCKKHglRGMRWKCRVCFDYDLCTQCYMHNKHD 125
Cdd:cd02337     3 CNECKHH--VETRWHCTVCEDYDLCITCYNTKNHP 35
RING-HC_BIRC2_3_7 cd16713
RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar ...
830-877 1.40e-04

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: 40.53  E-value: 1.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1595776923 830 EAAECLVCSELALLILFSPCQHRTVCEECARRMKKCIRCQVVISKKLR 877
Cdd:cd16713     6 EERTCKVCMDKEVSIVFIPCGHLVVCTECAPSLRKCPICRATIKGTVR 53
RING-HC_BIRC4_8 cd16714
RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP ...
834-877 1.52e-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: 40.51  E-value: 1.52e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1595776923 834 CLVCSELALLILFSPCQHRTVCEECARRMKKCIRCQVVISKKLR 877
Cdd:cd16714    17 CKICMDRNISIVFIPCGHLVTCKQCAEALDKCPICCTVITFKQK 60
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
488-605 1.59e-04

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 45.56  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 488 RASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGtrSTALHVAVQRGFLEVVKILCERGCDVNlpdAHA--- 564
Cdd:cd22193    35 KALLNLNPGTNDTIRILLDIAEKTDNLKRFINAEYTDEYYEG--QTALHIAIERRQGDIVALLVENGADVH---AHAkgr 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776923 565 --------------DTPLhsAISAGAGASSIVEVLTEVP--GIDVTATNSQGFTLLH 605
Cdd:cd22193   110 ffqpkyqgegfyfgELPL--SLAACTNQPDIVQYLLENEhqPADIEAQDSRGNTVLH 164
RING-HC_CARP1 cd16706
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 1 (CARP1) ...
908-956 1.61e-04

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: 40.39  E-value: 1.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776923 908 EERITCPICIDSHIRLVF-QCGHG-ACAPCGAALNACPICRQPIRDRIQIF 956
Cdd:cd16706     2 SDDNLCRICMDAVIDCVLlECGHMvTCTKCGKRMSECPICRQYVVRAVHVF 52
RING-HC_TRIM43-like_C-IV cd16603
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, ...
911-952 1.67e-04

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, TRIM51, TRIM64 and similar proteins; The family includes a group of closely related uncharacterized tripartite motif-containing proteins, TRIM43, TRIM43B, TRIM48/RNF101, TRIM49/RNF18, TRIM49B, TRIM49C/TRIM49L2, TRIM49D/TRIM49L, TRIM51/SPRYD5, TRIM64, TRIM64B, and TRIM64C, whose biological function remain unclear. TRIM49, also known as testis-specific RING-finger protein, has moderate similarity with SS-A/Ro52 antigen, suggesting it may be one of the target proteins of autoantibodies in the sera of patients with these autoimmune disorders. All family members 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 as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. In RBCC region, they all have a C3HC4-type RING-HC finger.


Pssm-ID: 438265 [Multi-domain]  Cd Length: 59  Bit Score: 40.54  E-value: 1.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1595776923 911 ITCPICIDSHIRLV-FQCGHGACAPC-------GAALNACPICRQPIRDR 952
Cdd:cd16603     5 LTCPICMNYFIDPVtIDCGHSFCRPClylnwqdIPFLAQCPECRKTTEQR 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
633-663 1.79e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 1.79e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1595776923  633 DGFTALHLAALNNHREVAQVLIREGRcDVNV 663
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA-DINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
633-666 2.00e-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: 39.58  E-value: 2.00e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1595776923 633 DGFTALHLAAL-NNHREVAQVLIREGrCDVNVRNR 666
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKG-ADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
531-575 2.47e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 2.47e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1595776923 531 RSTALHVAVQRGFLEVVKILCERGCDVNLPDAHADTPLHSAISAG 575
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
428-492 2.72e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.86  E-value: 2.72e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595776923 428 SDPEHPGRLVVEAALGNVARALDLLRRHPEQVDTKN-QGRTALQVAAYLGQVELVRLLLQARASMD 492
Cdd:PLN03192  617 SDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDhQGATALQVAMAEDHVDMVRLLIMNGADVD 682
mRING-HC-C3HC5_CGRF1 cd16787
Modified RING finger, HC subclass (C3HC5-type), found in cell growth regulator with RING ...
833-869 2.82e-04

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: 39.27  E-value: 2.82e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1595776923 833 ECLVCSELALLILFSPCQHRTVCEECARRMKKCIRCQ 869
Cdd:cd16787     2 DCVVCQNAPVNRVLLPCRHACVCDECFKRLQRCPMCR 38
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
533-559 2.84e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 2.84e-04
                           10        20
                   ....*....|....*....|....*..
gi 1595776923  533 TALHVAVQRGFLEVVKILCERGCDVNL 559
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
533-561 3.17e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 3.17e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1595776923 533 TALHVAV-QRGFLEVVKILCERGCDVNLPD 561
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
670-714 4.86e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 4.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1595776923 670 SPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVALQRHQL 714
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNV 47
RING-HC_UNK-like cd16614
RING finger, HC subclass, found in RING finger protein unkempt (UNK), unkempt-like (UNKL), and ...
833-869 6.29e-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: 38.31  E-value: 6.29e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1595776923 833 ECLVCSELALLILFSPCQHRTVCEECARRMKKCIRCQ 869
Cdd:cd16614     2 KCMKCEERNRSVAVLPCQHYVLCEQCAETATECPYCH 38
Ank_4 pfam13637
Ankyrin repeats (many copies);
636-688 7.35e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 7.35e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1595776923 636 TALHLAALNNHREVAQVLIrEGRCDVNVRNRKLQSPLHLAVQQAHLGLVPLLV 688
Cdd:pfam13637   3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
913-945 8.04e-04

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 404756 [Multi-domain]  Cd Length: 40  Bit Score: 37.80  E-value: 8.04e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1595776923 913 CPICID--SHIRLVFQCGHGACAPCGA----ALNACPIC 945
Cdd:pfam13923   2 CPICMDmlKDPSTTTPCGHVFCQDCILralrAGNECPLC 40
RING-HC_TRIM32_C-VII cd16587
RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar ...
912-947 8.90e-04

RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar proteins; TRIM32, also known as 72 kDa Tat-interacting protein, zinc finger protein HT2A, or BBS11, is an E3 ubiquitin-protein ligase that promotes degradation of several targets, including actin, PIASgamma, Abl interactor 2, dysbindin, X-linked inhibitor of apoptosis (XIAP), p73 transcription factor, thin filaments and Z-bands during fasting. It plays important roles in neuronal differentiation of neural progenitor cells, as well as in controlling cell fate in skeletal muscle progenitor cells. It reduces PI3K-Akt-FoxO signaling in muscle atrophy by promoting plakoglobin-PI3K dissociation. It also functions as a pluripotency-reprogramming roadblock that facilitates cellular transition towards differentiation by modulating the levels of Oct4 and cMyc. Moreover, TRIM32 is an intrinsic influenza A virus (IAV) restriction factor which senses and targets the polymerase basic protein 1 (PB1) for ubiquitination and protein degradation. It also plays a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo, binds specifically to the activation domain of HIV-1 Tat, and can also interact with the HIV-2 and EIAV Tat proteins in vivo. Furthermore, TRIM32 regulates myoblast proliferation by controlling turnover of NDRG2 (N-myc downstream-regulated gene). It negatively regulates tumor suppressor p53 to promote tumorigenesis. It also facilitates degradation of MYCN on spindle poles and induces asymmetric cell division in human neuroblastoma cells. In addition, TRIM32 plays important roles in regulation of hyperactivities and positively regulates the development of anxiety and depression disorders induced by chronic stress. It also plays a role in regeneration by affecting satellite cell cycle progression via modulation of the SUMO ligase PIASy (PIAS4). Defects in TRIM32 leads to limb-girdle muscular dystrophy type 2H (LGMD2H), sarcotubular myopathies (STM) and Bardet-Biedl syndrome. TRIM32 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is 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 domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The NHL domain mediates the interaction with Argonaute proteins and consequently allows TRIM32 to modulate the activity of certain miRNAs.


Pssm-ID: 438249 [Multi-domain]  Cd Length: 51  Bit Score: 38.15  E-value: 8.90e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1595776923 912 TCPICIDS-----HIRLVFQCGHGACAPCGAALNA--------CPICRQ 947
Cdd:cd16587     2 ECPICLESfdegqLRPKLLHCGHTICEQCLEKLLAslsingvrCPFCRK 50
PHA02875 PHA02875
ankyrin repeat protein; Provisional
466-695 9.01e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 9.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 466 RTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVAVQRGFLE 545
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 546 VVKILCERGC---DVNLPDahADTPLHSAIsagagASSIVEVLTEV--PGIDVTATNSQGFTLLHHASLKGHVLAVrKIL 620
Cdd:PHA02875   83 AVEELLDLGKfadDVFYKD--GMTPLHLAT-----ILKKLDIMKLLiaRGADPDIPNTDKFSPLHLAVMMGDIKGI-ELL 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595776923 621 ARARQLVDAKKEDGFTALHLAALNNHREVAQVLIREGRCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVN 695
Cdd:PHA02875  155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
RING-HC_TRIM4_C-IV cd16590
RING finger, HC subclass, found in tripartite motif-containing protein TRIM4 and similar ...
907-948 9.16e-04

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: 38.47  E-value: 9.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1595776923 907 MEERITCPICIDSHIRLV-FQCGHGACAPC-------GAALNACPICRQP 948
Cdd:cd16590     3 IQEELTCPICLDYFQDPVsIECGHNFCRGClhrnwapGGGPFPCPECRHP 52
ZZ_ADA2 cd02335
Zinc finger, ZZ type. Zinc finger present in ADA2, a putative transcriptional adaptor, and ...
89-131 1.01e-03

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


Pssm-ID: 239075 [Multi-domain]  Cd Length: 49  Bit Score: 38.04  E-value: 1.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1595776923  89 IICDCCKKHGLRGMRWKCRVCFDYDLCTQCY----MHNKHDLTHAFE 131
Cdd:cd02335     1 YHCDYCSKDITGTIRIKCAECPDFDLCLECFsagaEIGKHRNDHNYR 47
RING-HC_DTX3-like cd16506
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like ...
912-946 1.05e-03

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like (DTX3L) and similar proteins; This subfamily contains Deltex3 (DTX3) and Deltex-3-like (DTX3L), both of which are E3 ubiquitin-protein ligases belonging to the Deltex (DTX) family. DTX3, also known as RING finger protein 154 (RNF154), has a biological function that remains unclear. DTX3L, also known as B-lymphoma- and BAL-associated protein (BBAP) or Rhysin-2 (Rhysin2), regulates endosomal sorting of the G protein-coupled receptor CXCR4 from endosomes to lysosomes. It also regulates subcellular localization of its partner protein, B aggressive lymphoma (BAL), by a dynamic nucleocytoplasmic trafficking mechanism. In contrast to other DTXs, both DTX3 and DTX3L contain a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. DTX3L can associate with DTX1 through its unique N termini and further enhance self-ubiquitination.


Pssm-ID: 438169 [Multi-domain]  Cd Length: 45  Bit Score: 37.73  E-value: 1.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1595776923 912 TCPICIDS-HIRLVFQ-CGHGACAPC-GAAL---NACPICR 946
Cdd:cd16506     2 TCPICLDEiQNKKTLEkCKHSFCEDCiDRALqvkPVCPVCG 42
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
633-663 1.06e-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: 37.24  E-value: 1.06e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1595776923 633 DGFTALHLAALNNHREVAQVLIREGrCDVNV 663
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENG-ADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
591-641 1.22e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776923 591 IDVTATNSQGFTLLHHASLKGHVLAVRKILARaRQLVDAKKEDGFTALHLA 641
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
mRING-HC-C3HC5_MAPL cd16648
Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase ...
913-956 1.47e-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: 37.45  E-value: 1.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1595776923 913 CPICIDSHIRLVF-QCGHG-ACAPCGAALNA---CPICRQPIRDRIQIF 956
Cdd:cd16648     4 CVICLSNPRSCVFlECGHVcSCIECYEALPSpkkCPICRSFIKRVVPLY 52
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
639-708 1.51e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 1.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 639 HLAALNNhrEVAQVLIREGRCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVA 708
Cdd:PTZ00322   88 QLAASGD--AVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
470-550 1.92e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 470 QVAAYLGQVEL-----------VRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVA 538
Cdd:PTZ00322   76 PVVAHMLTVELcqlaasgdavgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
                          90
                  ....*....|..
gi 1595776923 539 VQRGFLEVVKIL 550
Cdd:PTZ00322  156 EENGFREVVQLL 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
484-538 1.93e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1595776923 484 LLQAR-ASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGCAVDARNGTRSTALHVA 538
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
RING-HC_IAPs cd16510
RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently ...
834-868 2.12e-03

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: 36.85  E-value: 2.12e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1595776923 834 CLVCSELALLILFSPCQHRTVCEECARRMKKCIRC 868
Cdd:cd16510     4 CKICMDREVNIVFLPCGHLVTCAQCAASLRKCPIC 38
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
465-605 2.17e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.79  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 465 GRTALQVAA-YL--GQVELVRLLLQARASMDLPDDegntvlhytamgnqpeatrvLLSAGCAVDARNGtrSTALHVAVQR 541
Cdd:cd21882    26 GKTCLHKAAlNLndGVNEAIMLLLEAAPDSGNPKE--------------------LVNAPCTDEFYQG--QTALHIAIEN 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595776923 542 GFLEVVKILCERGCDVNLP---DAHADTP--------LHSAISAGAGASSIVEVLTEVPG--IDVTATNSQGFTLLH 605
Cdd:cd21882    84 RNLNLVRLLVENGADVSARatgRFFRKSPgnlfyfgeLPLSLAACTNQEEIVRLLLENGAqpAALEAQDSLGNTVLH 160
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
533-558 2.40e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 2.40e-03
                          10        20
                  ....*....|....*....|....*.
gi 1595776923 533 TALHVAVQRGFLEVVKILCERGCDVN 558
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
RING-HC_MIP1-like cd23128
RING finger, HC subclass, found in Arabidopsis thaliana MND1-interacting protein 1 (MIP1) and ...
832-877 2.54e-03

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: 37.10  E-value: 2.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776923 832 AECLVCSELALLILFSPCQHRTVCEECA-----RRMKKCIRCQVVISKKLR 877
Cdd:cd23128     4 RECVMCMEEERSVVFLPCAHQVVCSGCNdlhekKGMRECPSCRGEIQERIR 54
RING-HC_MYLIP cd16523
RING finger, HC subclass, found in myosin regulatory light chain interacting protein (MYLIP) ...
909-954 2.57e-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: 36.78  E-value: 2.57e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1595776923 909 ERITCPICIDSHIRLVF-QCGHGACA-PCGAALNACPICRQPIrDRIQ 954
Cdd:cd16523     1 EAMLCMVCCEEEINSAFcPCGHMVCCeSCAAQLQSCPVCRSRV-EHVQ 47
RING-HC_RNF4 cd16533
RING finger, HC subclass, found in RING finger protein 4 (RNF4) and similar proteins; RNF4, ...
911-952 2.74e-03

RING finger, HC subclass, found in RING finger protein 4 (RNF4) and similar proteins; RNF4, also known as small nuclear ring finger protein (SNURF), is a SUMO-targeted E3 ubiquitin-protein ligase with a pivotal function in the DNA damage response (DDR) by interacting with the deubiquitinating enzyme ubiquitin-specific protease 11 (USP11), a known DDR-component, and further facilitating DNA repair. It plays a novel role in preventing the loss of intact chromosomes and ensures the maintenance of chromosome integrity. Moreover, RNF4 is responsible for the UbcH5A-catalyzed formation of K48 chains that target SUMO-modified promyelocytic leukemia (PML) protein for proteasomal degradation in response to arsenic treatment. It also interacts with telomeric repeat binding factor 2 (TRF2) in a small ubiquitin-like modifier (SUMO)-dependent manner and preferentially targets SUMO-conjugated TRF2 for ubiquitination through SUMO-interacting motifs (SIMs). Furthermore, RNF4 can form a complex with a Ubc13-ubiquitin conjugate and Ube2V2. It catalyzes K63-linked polyubiquitination by the Ube2V2-Ubc13 (ubiquitin-loaded) complex. Meanwhile, RNF4 negatively regulates nuclear factor kappa B (NF-kappaB) signaling by down-regulating transforming growth factor beta (TGF-beta)-activated kinase 1 (TAK1)-TAK1-binding protein2 (TAB2). RNF4 contains four SIMs followed by a C3HC4-type RING-HC finger at the C-terminus.


Pssm-ID: 438195 [Multi-domain]  Cd Length: 57  Bit Score: 36.80  E-value: 2.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1595776923 911 ITCPICIDSHIRLV--------FQCGHGACAPC--GAALNA--CPICRQPIRDR 952
Cdd:cd16533     4 VSCPICMDGYSEIVqsgrlivsTECGHVFCSQClrDSLKNAntCPTCRKKLNHK 57
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
243-742 3.00e-03

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 41.78  E-value: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923  243 PAELQRRVSADGQPFQRGDKVKCLLDTDVLRDMQEGHGGWNPRMAEFIGQM------GTVHRITDRGDVRVQFNHETRWT 316
Cdd:COG3321    854 PGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALaaallaLAAAAAAALALAAAALAALLALV 933
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923  317 FHPGALTKHNSFWVGDVVRVIGDLDTVKRLQAGHGEWTDDMAPALGRVGKVVKVFGDGNLRVAVGGQRWTFSPSCLVAYR 396
Cdd:COG3321    934 ALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLA 1013
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923  397 PEEDANLDVAERARENKSSLSVALDKLRTQKSDPEHPGRLVVEAALGNVARALDLLRRHPEQVDTKNQGRTALQVAAYLG 476
Cdd:COG3321   1014 AAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAA 1093
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923  477 QVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGcAVDARNGTRSTALHVAVQRGFLEVVKILCERGCD 556
Cdd:COG3321   1094 ALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAA-ALAAAAAAAAALALAAAAAALAAALAAALLAAAA 1172
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923  557 VNLPDAHADTPLHSAISAGAGASSIVEVLTEVPGIDVTATNSQGFTLLHHASLKGHVLAVRKILARARQLVDAKKEDGFT 636
Cdd:COG3321   1173 LLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAA 1252
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923  637 ALHLAALNNHREVAQVLIREGRCDVNVRNRKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVALQRHQLLP 716
Cdd:COG3321   1253 AALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAA 1332
                          490       500
                   ....*....|....*....|....*.
gi 1595776923  717 LVADRAGGDPGPLQLLSRLQASGLPG 742
Cdd:COG3321   1333 LAAAVAAALALAAAAAAAAAAAAAAA 1358
PHA02736 PHA02736
Viral ankyrin protein; Provisional
593-691 3.10e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.09  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 593 VTATNSQGFTLLHHASLKGHVLAVRKI--LARARQLVDAKKE-DGFTALHLAALNNHREVAQVLIREGRCDVNVRNRKLQ 669
Cdd:PHA02736   48 VLEYNRHGKQCVHIVSNPDKADPQEKLklLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFK 127
                          90       100
                  ....*....|....*....|..
gi 1595776923 670 SPLHLAVQQAHLGLVPLLVDAG 691
Cdd:PHA02736  128 TPYYVACERHDAKMMNILRAKG 149
RING-HC_TRIM7-like_C-IV cd16594
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and ...
909-952 3.16e-03

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: 36.90  E-value: 3.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1595776923 909 ERITCPICIDSHIRLVF-QCGHGACAPC-------GAALNACPICRQPIRDR 952
Cdd:cd16594     4 EELTCPICLDYFTDPVTlDCGHSFCRACiarcweePETSASCPQCRETCPQR 55
RING-HC_CblA-like cd16501
RING finger, HC subclass, found in Dictyostelium discoideum Cbl-like protein A (CblA) and ...
828-877 3.24e-03

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: 36.70  E-value: 3.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1595776923 828 GPEAAECLVCSELALLILFSPCQHRTVCEECARRMKKCIRCQVVISKKLR 877
Cdd:cd16501     2 GADADLCVVCMDAPIDTVFLECGHLACCRLCSKRLRVCPICRQPISRVVR 51
RING-HC_MmTRIM43-like cd23133
RING finger, HC subclass, found in Mus musculus tripartite motif-containing protein 43 (TRIM43) ...
908-952 3.30e-03

RING finger, HC subclass, found in Mus musculus tripartite motif-containing protein 43 (TRIM43) and similar propteins; This subfamily includes TRIM43A, TRIM43B and TRIM43C, which are expressed specifically in mouse preimplantation embryos. They contain a typical C3HC4-type RING-HC finger.


Pssm-ID: 438495 [Multi-domain]  Cd Length: 57  Bit Score: 36.81  E-value: 3.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1595776923 908 EERITCPICIDSHIRLVF-QCGHGACAPCG-------AALNACPICRQPIRDR 952
Cdd:cd23133     1 EETLTCSICQGIFMNPVYlRCGHKFCEACLllfqediKFPAYCPMCRQPFNQE 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
464-496 3.36e-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: 36.11  E-value: 3.36e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1595776923 464 QGRTALQVAAY-LGQVELVRLLLQARASMDLPDD 496
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
RING-HC_MEX3B cd16721
RING finger, HC subclass, found in RNA-binding protein MEX3B; MEX3B, also known as RING finger ...
833-877 3.39e-03

RING finger, HC subclass, found in RNA-binding protein MEX3B; MEX3B, also known as RING finger and KH domain-containing protein 3 (RKHD3), or RING finger protein 195 (RNF195), is an RNA-binding phosphoprotein that localizes in P-bodies and stress granules, which are two structures involved in the storage and turnover of mRNAs. It regulates the spatial organization of the Rap1 pathway that orchestrates Sertoli cell functions. It has a 3' long conserved untranslated region (3'LCU)-mediated fine-tuning system for mRNA regulation in early vertebrate development such as anteroposterior (AP) patterning and signal transduction. MEX3B contains two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. Like other MEX-3 family proteins, MEX3B shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway.


Pssm-ID: 438381 [Multi-domain]  Cd Length: 58  Bit Score: 36.58  E-value: 3.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1595776923 833 ECLVCSELALLILFSPCQHRTVCEECARRM-----KKCIRCQVVISKKLR 877
Cdd:cd16721     6 DCSICFESEVIAALVPCGHNLFCMECANRIceknePQCPVCHAAVTQAIR 55
ZZ_UBA_plant cd02342
Zinc finger, ZZ type. Zinc finger present in plant ubiquitin-associated (UBA) proteins. The ZZ ...
89-127 3.56e-03

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


Pssm-ID: 239082  Cd Length: 43  Bit Score: 36.02  E-value: 3.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1595776923  89 IICDCCKKHGLRGMRWKCRVCFDYDLCTQCY--MHNKHDLT 127
Cdd:cd02342     1 IQCDGCGVLPITGPRYKSKVKEDYDLCTICFsrMGNEGEYT 41
RING-HC_TRIM26_C-IV cd16598
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar ...
907-950 3.66e-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: 36.68  E-value: 3.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1595776923 907 MEERITCPICIDsHIR--LVFQCGHGACAPC---------GAALNACPICRQPIR 950
Cdd:cd16598     1 LEEEVTCSICLD-YLRdpVTIDCGHNFCRSCitdycpisgGHERPVCPLCRKPFK 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
600-708 3.90e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.22  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 600 GFTLLHHASLKGHV---LAVRKILARAR-----QLVDAKKEDGF----TALHLAALNNHREVAQVLIREGrCDVNVRN-- 665
Cdd:TIGR00870  82 GDTLLHAISLEYVDaveAILLHLLAAFRksgplELANDQYTSEFtpgiTALHLAAHRQNYEIVKLLLERG-ASVPARAcg 160
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1595776923 666 ------------RKLQSPLHLAVQQAHLGLVPLLVDAGCSVNTEDEEGDTALHVA 708
Cdd:TIGR00870 161 dffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLL 215
Ank_4 pfam13637
Ankyrin repeats (many copies);
566-613 4.20e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 4.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1595776923 566 TPLHSAisAGAGASSIVEVLTEvPGIDVTATNSQGFTLLHHASLKGHV 613
Cdd:pfam13637   3 TALHAA--AASGHLELLRLLLE-KGADINAVDGNGETALHFAASNGNV 47
Ank_5 pfam13857
Ankyrin repeats (many copies);
553-607 5.07e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 5.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1595776923 553 RGCDVNLPDAHADTPLHSAISagAGASSIVEVLTEvPGIDVTATNSQGFTLLHHA 607
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAK--YGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
RING-HC_RNF10 cd16536
RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 ...
911-950 5.52e-03

RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 is an E3 ubiquitin-protein ligase that interacts with mesenchyme Homeobox 2 (MEOX2) transcription factor, a regulator of the proliferation, differentiation and migration of vascular smooth muscle cells and cardiomyocytes; it enhances Meox2 activation of the p21 promoter. It also regulates the expression of myelin-associated glycoprotein (MAG) genes and is required for myelin production in Schwann cells of the peripheral nervous system. Moreover, RNF10 regulates retinoic acid-induced neuronal differentiation and the cell cycle exit of P19 embryonic carcinoma cells. RNF10 contains a C3HC4-type RING-HC finger and three putative nuclear localization signals.


Pssm-ID: 438198 [Multi-domain]  Cd Length: 54  Bit Score: 36.06  E-value: 5.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1595776923 911 ITCPICIDSHI--RLVfQCGHGACAPC--------GAALNACPICRQPIR 950
Cdd:cd16536     1 PQCPICLEPPVapRIT-RCGHIFCWPCilrylslsEKKWRKCPICFESIH 49
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
912-945 5.82e-03

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: 35.54  E-value: 5.82e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1595776923 912 TCPICIDSHIRLVF-QCGHGACAPCGAAL-----NACPIC 945
Cdd:cd16449     2 ECPICLERLKDPVLlPCGHVFCRECIRRLlesgsIKCPIC 41
RING-HC_XBAT35-like cd23129
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and ...
912-956 6.29e-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: 35.70  E-value: 6.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776923 912 TCPICIDSHIRLV-FQCGH-GACAPCGAAL----NACPICRQPIRDRIQIF 956
Cdd:cd23129     4 ECVVCMDAPRDAVcVPCGHvAGCMSCLKALmqssPLCPICRAPVRQVIKVY 54
RING-HC_MYLIP cd16523
RING finger, HC subclass, found in myosin regulatory light chain interacting protein (MYLIP) ...
830-869 6.49e-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: 35.62  E-value: 6.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1595776923 830 EAAECLVCSELALLILFSPCQHRTVCEECARRMKKCIRCQ 869
Cdd:cd16523     1 EAMLCMVCCEEEINSAFCPCGHMVCCESCAAQLQSCPVCR 40
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
533-605 6.54e-03

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 40.17  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 533 TALHVAVQRGFLEVVKILCERGCDVNlpdAHADTPLHSAISAGAG---------------ASSIVEVLTEVP--GIDVTA 595
Cdd:cd22196    96 TALHIAIERRNMHLVELLVQNGADVH---ARASGEFFKKKKGGPGfyfgelplslaactnQLDIVKFLLENPhsPADISA 172
                          90
                  ....*....|
gi 1595776923 596 TNSQGFTLLH 605
Cdd:cd22196   173 RDSMGNTVLH 182
PHA02859 PHA02859
ankyrin repeat protein; Provisional
478-602 6.94e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 6.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 478 VELVRLLLQARASMD-LPDDEGNTVLHYTAMGNQ---PEATRVLLSAGCAVDARNGTRSTALHVAVQRGF--LEVVKILC 551
Cdd:PHA02859   66 VEILKFLIENGADVNfKTRDNNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLLHMYMCNFNvrINVIKLLI 145
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1595776923 552 ERGCDVNLPDAHADTPLHSAISAGAgASSIVEVLTEVpGIDVTATNSQGFT 602
Cdd:PHA02859  146 DSGVSFLNKDFDNNNILYSYILFHS-DKKIFDFLTSL-GIDINETNKSGYN 194
RING-HC_RSPRY1 cd16566
RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) ...
913-949 7.21e-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: 35.41  E-value: 7.21e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1595776923 913 CPICIDSHIRLVFQ-CGH-GACAPCGAALNACPICRQPI 949
Cdd:cd16566     5 CTLCFDKVADTELRpCGHsGFCMECALQLETCPLCRQPI 43
RING-HC_RNF146 cd16546
RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins; ...
911-949 7.99e-03

RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins; RNF146, also known as dactylidin, or iduna, is a cytoplasmic E3 ubiquitin-protein ligase that is responsible for PARylation-dependent ubiquitination (PARdU). It displays neuroprotective property due to its inhibition of Parthanatos, a PAR dependent cell death, via binding with Poly(ADP-ribose) (PAR). It also modulates PAR polymerase-1 (PARP-1)-mediated oxidative cell injury in cardiac myocytes. Moreover, RNF146 mediates tankyrase-dependent degradation of axin, thereby positively regulating Wnt signaling. It also facilitates DNA repair and protects against cell death induced by DNA damaging agents or gamma-irradiation by translocating to the nucleus after cellular injury and promoting the ubiquitination and degradation of various nuclear proteins involved in DNA damage repair. Furthermore, RNF146 is implicated in neurodegenerative disease and cancer development. It regulates the development and progression of non-small cell lung cancer (NSCLC) by enhancing cell growth, invasion, and survival. RNF146 contains an N-terminal C3HC4-type RING-HC finger followed by a WWE domain with a poly(ADP-ribose) (PAR) binding motif at the tail.


Pssm-ID: 438208 [Multi-domain]  Cd Length: 50  Bit Score: 35.44  E-value: 7.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1595776923 911 ITCPICIDSHIRLV-FQCGHGACAPC--GAALNA--CPICRQPI 949
Cdd:cd16546     1 PECPICLQTCIHPVkLPCGHIFCYLCvkGVAWQSkrCALCRQEI 44
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
398-545 8.91e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.88  E-value: 8.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 398 EEDANLDVAERARENKSSLSVALDK-LRTQKS-DPEHPGRLVVE----AALGNVARALDLLRRHPEQVDTKNQGRTALQV 471
Cdd:PTZ00322   42 EEIARIDTHLEALEATENKDATPDHnLTTEEViDPVVAHMLTVElcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHI 121
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595776923 472 AAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRvLLSAGCAVDARNGTRSTALHVAVQRGFLE 545
Cdd:PTZ00322  122 ACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ-LLSRHSQCHFELGANAKPDSFTGKPPSLE 194
PHA03100 PHA03100
ankyrin repeat protein; Provisional
444-530 9.41e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.65  E-value: 9.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595776923 444 NVARALDLLRRHPEQVDTKNQ-GRTALQVAAYLGQVELVRLLLQARASMDLPDDEGNTVLHYTAMGNQPEATRVLLSAGC 522
Cdd:PHA03100  170 NAKNRVNYLLSYGVPINIKDVyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249

                  ....*...
gi 1595776923 523 AVDARNGT 530
Cdd:PHA03100  250 SIKTIIET 257
RING-HC_TRIM50_like_C-IV cd16605
RING finger, HC subclass, found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 ...
911-947 9.85e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 and similar proteins; TRIM50 is a stomach-specific E3 ubiquitin-protein ligase, encoded by the Williams-Beuren syndrome (WBS) TRIM50 gene, which regulates vesicular trafficking for acid secretion in gastric parietal cells. It colocalizes, interacts with, and increases the level of p62/SQSTM1, a multifunctional adaptor protein implicated in various cellular processes including the autophagy clearance of polyubiquitinated protein aggregates. It also promotes the formation and clearance of aggresome-associated polyubiquitinated proteins through the interaction with histone deacetylase 6 (HDAC6), a tubulin specific deacetylase that regulates microtubule-dependent aggresome formation. TRIM50 can be acetylated by PCAF and p300. TRIM50 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. This subfamily also includes two paralogs of TRIM50, tripartite motif-containing protein 73 (TRIM73), also known as tripartite motif-containing protein 50B (TRIM50B), and tripartite motif-containing protein 74 (TRIM74), also known as tripartite motif-containing protein 50C (TRIM50C), both of which are WBS-related genes encoding proteins that may also act as E3 ligases. In contrast with TRIM50, TRIM73 and TRIM74 belong to the C-V subclass of TRIM family of proteins that are defined by N-terminal RBCC domains only.


Pssm-ID: 438267 [Multi-domain]  Cd Length: 45  Bit Score: 35.12  E-value: 9.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1595776923 911 ITCPICIDSHIR-LVFQCGHGACAPCGAALNA-------CPICRQ 947
Cdd:cd16605     1 LLCPICLEVFKEpLMLQCGHSYCKSCLVSLSGeldgqllCPVCRQ 45
 
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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