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Conserved domains on  [gi|163644309|ref|NP_031490.2|]
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baculoviral IAP repeat-containing protein 3 [Mus musculus]

Protein Classification

CARD_BIRC2_BIRC3 and RING-HC_BIRC2_3_7 domain-containing protein (domain architecture ID 12198268)

protein containing domains BIR, UBA_BIRC2_3, CARD_BIRC2_BIRC3, and RING-HC_BIRC2_3_7

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
440-528 5.53e-48

Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, BIRC2 (c-IAP1) and BIRC3 (c-IAP2); Caspase activation and recruitment domain (CARD) similar to those found in Baculoviral IAP repeat (BIR)-containing protein 2 (BIRC2) or cellular Inhibitor of Apoptosis Protein 1 (c-IAP1), and BIRC3 (or c-IAP2). IAPs are anti-apoptotic proteins that contain at least one BIR domain. Most IAPs also contain a C-terminal RING domain. In addition, both BIRC2 and BIRC3 contain a CARD. BIRC2 and BIRC3, through their binding with TRAF (TNF receptor-associated factor) 2, are recruited to TNFR-1/2 signaling complexes, where they regulate caspase-8 activity. They also play important roles in pro-survival NF-kB signaling pathways. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260038  Cd Length: 94  Bit Score: 162.23  E-value: 5.53e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644309 440 SDDLALIRKNKMVLFQHLTCVTPMLYCLLSARAITEQECNAVKQKPHT-LQASTLIDTVLAKGNTAATSFRNSLREIDPA 518
Cdd:cd08329    5 SDDLSLIRKNRMALFQHLTCVLPILDHLLSANVITEQEYDVIKQKTQTpLQARELIDTILVKGNAAAEVFRNCLKEIDVV 84
                         90
                 ....*....|
gi 163644309 519 LYRDIFVQQD 528
Cdd:cd08329   85 LYRDLFVQKS 94
RING-HC_BIRC2_3_7 cd16713
RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar ...
549-602 4.79e-35

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 the substrates involved in apoptosis, nuclear factor-kappaB (NF-kappaB) signaling, and oncogenesis. Unlike other apoptosis proteins (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 binds 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), or kidney inhibitor of apoptosis protein (KIAP), or 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: 319627 [Multi-domain]  Cd Length: 54  Bit Score: 125.65  E-value: 4.79e-35
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 163644309 549 LQEERMCKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICRGTIKGTVRTFLS 602
Cdd:cd16713    1 LQEERTCKVCMDKEVSIVFVPCGHLAVCQECAPSLRKCPICRAKIKGTVRTFLS 54
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
254-324 7.59e-33

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


:

Pssm-ID: 197595  Cd Length: 71  Bit Score: 120.11  E-value: 7.59e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 163644309   254 THAARIRTFSNWPSSALVHSQELASAGFYYTGHSDDVKCFCCDGGLRCWESGDDPWVEHAKWFPRCEYLLR 324
Cdd:smart00238   1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVRN 71
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
168-236 1.07e-29

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


:

Pssm-ID: 197595  Cd Length: 71  Bit Score: 111.26  E-value: 1.07e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644309   168 TEKARLLTYETWP-LSFLSPAKLAKAGFYYIGPGDRVACFACDGKLSNWERKDDAMSEHQRHFPSCPFLK 236
Cdd:smart00238   1 SEEARLKTFQNWPyNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVR 70
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
28-97 8.86e-29

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


:

Pssm-ID: 197595  Cd Length: 71  Bit Score: 108.94  E-value: 8.86e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644309    28 CELYRLSTYSAFPRGVPVSERSLARAGFYYTGANDKVKCFCCGLMLDNWKQGDSPMEKHRKLYPSCNFVQ 97
Cdd:smart00238   1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVR 70
UBA_BIRC2_3 cd14394
UBA domain found in baculoviral IAP repeat-containing protein BIRC2, BIRC3 and similar ...
376-425 4.70e-23

UBA domain found in baculoviral IAP repeat-containing protein BIRC2, BIRC3 and similar proteins; The subfamily includes cellular inhibitor of apoptosis protein 1 (c-IAP1) and c-IAP2. c-IAPs function as ubiquitin E3 ligases that mediate the ubiquitination of the substrates involved in apoptosis, nuclear factor-kappaB (NF-kappaB)signaling, and oncogenesis. Unlike other apoptosis proteins (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 called 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 called 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 binds polyubiquitin (polyUb), a caspase activation and recruitment domain (CARD) that serves as a protein interaction surface, and a RING domain at the carboxyl terminus that is required for ubiquitin ligase activity.


:

Pssm-ID: 270577  Cd Length: 50  Bit Score: 91.90  E-value: 4.70e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 163644309 376 MSTPVVKAALEMGFSRSLVRQTVQWQILATGENYRTVSDLVIGLLDAEDE 425
Cdd:cd14394    1 MNTPVVKSALEMGFNRRLVKQTVQSKILTSGENYKTVNDLVSDLLSAEDE 50
 
Name Accession Description Interval E-value
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
440-528 5.53e-48

Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, BIRC2 (c-IAP1) and BIRC3 (c-IAP2); Caspase activation and recruitment domain (CARD) similar to those found in Baculoviral IAP repeat (BIR)-containing protein 2 (BIRC2) or cellular Inhibitor of Apoptosis Protein 1 (c-IAP1), and BIRC3 (or c-IAP2). IAPs are anti-apoptotic proteins that contain at least one BIR domain. Most IAPs also contain a C-terminal RING domain. In addition, both BIRC2 and BIRC3 contain a CARD. BIRC2 and BIRC3, through their binding with TRAF (TNF receptor-associated factor) 2, are recruited to TNFR-1/2 signaling complexes, where they regulate caspase-8 activity. They also play important roles in pro-survival NF-kB signaling pathways. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260038  Cd Length: 94  Bit Score: 162.23  E-value: 5.53e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644309 440 SDDLALIRKNKMVLFQHLTCVTPMLYCLLSARAITEQECNAVKQKPHT-LQASTLIDTVLAKGNTAATSFRNSLREIDPA 518
Cdd:cd08329    5 SDDLSLIRKNRMALFQHLTCVLPILDHLLSANVITEQEYDVIKQKTQTpLQARELIDTILVKGNAAAEVFRNCLKEIDVV 84
                         90
                 ....*....|
gi 163644309 519 LYRDIFVQQD 528
Cdd:cd08329   85 LYRDLFVQKS 94
RING-HC_BIRC2_3_7 cd16713
RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar ...
549-602 4.79e-35

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 the substrates involved in apoptosis, nuclear factor-kappaB (NF-kappaB) signaling, and oncogenesis. Unlike other apoptosis proteins (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 binds 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), or kidney inhibitor of apoptosis protein (KIAP), or 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: 319627 [Multi-domain]  Cd Length: 54  Bit Score: 125.65  E-value: 4.79e-35
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 163644309 549 LQEERMCKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICRGTIKGTVRTFLS 602
Cdd:cd16713    1 LQEERTCKVCMDKEVSIVFVPCGHLAVCQECAPSLRKCPICRAKIKGTVRTFLS 54
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
254-324 7.59e-33

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


Pssm-ID: 197595  Cd Length: 71  Bit Score: 120.11  E-value: 7.59e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 163644309   254 THAARIRTFSNWPSSALVHSQELASAGFYYTGHSDDVKCFCCDGGLRCWESGDDPWVEHAKWFPRCEYLLR 324
Cdd:smart00238   1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVRN 71
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
256-323 7.10e-32

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 117.37  E-value: 7.10e-32
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163644309 256 AARIRTFSNWPSSALVHSQELASAGFYYTGHSDDVKCFCCDGGLRCWESGDDPWVEHAKWFPRCEYLL 323
Cdd:cd00022    1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVL 68
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
258-323 6.08e-30

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteristically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 334196  Cd Length: 69  Bit Score: 112.00  E-value: 6.08e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644309  258 RIRTF-SNWPSSAL--VHSQELASAGFYYTGHSDDVKCFCCDGGLRCWESGDDPWVEHAKWFPRCEYLL 323
Cdd:pfam00653   1 RLATFkDNWPLSAKspPSPEELAEAGFYYTGTGDRVQCFYCGGELDGWEPGDDPWEEHKKHSPNCPFLK 69
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
168-236 1.07e-29

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


Pssm-ID: 197595  Cd Length: 71  Bit Score: 111.26  E-value: 1.07e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644309   168 TEKARLLTYETWP-LSFLSPAKLAKAGFYYIGPGDRVACFACDGKLSNWERKDDAMSEHQRHFPSCPFLK 236
Cdd:smart00238   1 SEEARLKTFQNWPyNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVR 70
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
170-236 3.37e-29

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 110.05  E-value: 3.37e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163644309 170 KARLLTYETWPLS-FLSPAKLAKAGFYYIGPGDRVACFACDGKLSNWERKDDAMSEHQRHFPSCPFLK 236
Cdd:cd00022    1 EARLKTFKNWPISlKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVL 68
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
28-97 8.86e-29

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


Pssm-ID: 197595  Cd Length: 71  Bit Score: 108.94  E-value: 8.86e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644309    28 CELYRLSTYSAFPRGVPVSERSLARAGFYYTGANDKVKCFCCGLMLDNWKQGDSPMEKHRKLYPSCNFVQ 97
Cdd:smart00238   1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVR 70
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
32-97 2.49e-28

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 107.35  E-value: 2.49e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 163644309  32 RLSTYSAFPRGVPVSERSLARAGFYYTGANDKVKCFCCGLMLDNWKQGDSPMEKHRKLYPSCNFVQ 97
Cdd:cd00022    3 RLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVL 68
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
172-236 1.76e-26

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteristically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 334196  Cd Length: 69  Bit Score: 102.37  E-value: 1.76e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644309  172 RLLTY-ETWPLSFL---SPAKLAKAGFYYIGPGDRVACFACDGKLSNWERKDDAMSEHQRHFPSCPFLK 236
Cdd:pfam00653   1 RLATFkDNWPLSAKsppSPEELAEAGFYYTGTGDRVQCFYCGGELDGWEPGDDPWEEHKKHSPNCPFLK 69
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
32-97 2.73e-26

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteristically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 334196  Cd Length: 69  Bit Score: 101.60  E-value: 2.73e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644309   32 RLSTY-SAFPRG--VPVSERSLARAGFYYTGANDKVKCFCCGLMLDNWKQGDSPMEKHRKLYPSCNFVQ 97
Cdd:pfam00653   1 RLATFkDNWPLSakSPPSPEELAEAGFYYTGTGDRVQCFYCGGELDGWEPGDDPWEEHKKHSPNCPFLK 69
UBA_BIRC2_3 cd14394
UBA domain found in baculoviral IAP repeat-containing protein BIRC2, BIRC3 and similar ...
376-425 4.70e-23

UBA domain found in baculoviral IAP repeat-containing protein BIRC2, BIRC3 and similar proteins; The subfamily includes cellular inhibitor of apoptosis protein 1 (c-IAP1) and c-IAP2. c-IAPs function as ubiquitin E3 ligases that mediate the ubiquitination of the substrates involved in apoptosis, nuclear factor-kappaB (NF-kappaB)signaling, and oncogenesis. Unlike other apoptosis proteins (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 called 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 called 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 binds polyubiquitin (polyUb), a caspase activation and recruitment domain (CARD) that serves as a protein interaction surface, and a RING domain at the carboxyl terminus that is required for ubiquitin ligase activity.


Pssm-ID: 270577  Cd Length: 50  Bit Score: 91.90  E-value: 4.70e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 163644309 376 MSTPVVKAALEMGFSRSLVRQTVQWQILATGENYRTVSDLVIGLLDAEDE 425
Cdd:cd14394    1 MNTPVVKSALEMGFNRRLVKQTVQSKILTSGENYKTVNDLVSDLLSAEDE 50
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
443-526 6.34e-22

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 334175  Cd Length: 85  Bit Score: 89.92  E-value: 6.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644309  443 LALIRKNKMVLFQHLTCVTPMLYCLLSARAITEQECNAVKQKPHTL-QASTLIDTVLAKGNTAATSFRNSLREIDPALYR 521
Cdd:pfam00619   1 LELLKKNREALVERLTTLDGLLDYLLEKNVLTEEEYEKIKANTTRLdKARELLDLVLKKGPEACQIFLQALKEGDPDLAS 80

                  ....*
gi 163644309  522 DIFVQ 526
Cdd:pfam00619  81 LLELL 85
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
551-594 1.05e-15

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 339001 [Multi-domain]  Cd Length: 48  Bit Score: 70.87  E-value: 1.05e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 163644309  551 EERMCKVCMDREVSIVFIPCGHLVVCKDCAPSLR----KCPICRGTIK 594
Cdd:pfam13920   1 EDRLCVICLDRPRNVVLLPCGHLCLCEECAERLRkkkkKCPICRQPIE 48
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
440-520 1.52e-07

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain.


Pssm-ID: 128424  Cd Length: 88  Bit Score: 49.26  E-value: 1.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644309   440 SDDLALIRKNKMVLFQHLTCVtPMLYCLLSARAITEQECNAVKQKPHTL-QASTLIDTVLAKGNTAATSFRNSLREIDPA 518
Cdd:smart00114   3 ERDKRLLRRNRVRLGEELGVD-GLLDYLVEKNVLTEKEIEAIKAATTKLrDKRELVDSLQKRGSQAFDTFLDSLQETDQK 81

                   ..
gi 163644309   519 LY 520
Cdd:smart00114  82 LA 83
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
555-589 2.03e-03

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 35.95  E-value: 2.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 163644309   555 CKVCMDR-EVSIVFIPCGHlVVCKDCAPSL-----RKCPIC 589
Cdd:smart00184   1 CPICLEEyLKDPVILPCGH-TFCRSCIRKWlesgnNTCPIC 40
 
Name Accession Description Interval E-value
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
440-528 5.53e-48

Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, BIRC2 (c-IAP1) and BIRC3 (c-IAP2); Caspase activation and recruitment domain (CARD) similar to those found in Baculoviral IAP repeat (BIR)-containing protein 2 (BIRC2) or cellular Inhibitor of Apoptosis Protein 1 (c-IAP1), and BIRC3 (or c-IAP2). IAPs are anti-apoptotic proteins that contain at least one BIR domain. Most IAPs also contain a C-terminal RING domain. In addition, both BIRC2 and BIRC3 contain a CARD. BIRC2 and BIRC3, through their binding with TRAF (TNF receptor-associated factor) 2, are recruited to TNFR-1/2 signaling complexes, where they regulate caspase-8 activity. They also play important roles in pro-survival NF-kB signaling pathways. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260038  Cd Length: 94  Bit Score: 162.23  E-value: 5.53e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644309 440 SDDLALIRKNKMVLFQHLTCVTPMLYCLLSARAITEQECNAVKQKPHT-LQASTLIDTVLAKGNTAATSFRNSLREIDPA 518
Cdd:cd08329    5 SDDLSLIRKNRMALFQHLTCVLPILDHLLSANVITEQEYDVIKQKTQTpLQARELIDTILVKGNAAAEVFRNCLKEIDVV 84
                         90
                 ....*....|
gi 163644309 519 LYRDIFVQQD 528
Cdd:cd08329   85 LYRDLFVQKS 94
RING-HC_BIRC2_3_7 cd16713
RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar ...
549-602 4.79e-35

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 the substrates involved in apoptosis, nuclear factor-kappaB (NF-kappaB) signaling, and oncogenesis. Unlike other apoptosis proteins (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 binds 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), or kidney inhibitor of apoptosis protein (KIAP), or 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: 319627 [Multi-domain]  Cd Length: 54  Bit Score: 125.65  E-value: 4.79e-35
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 163644309 549 LQEERMCKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICRGTIKGTVRTFLS 602
Cdd:cd16713    1 LQEERTCKVCMDKEVSIVFVPCGHLAVCQECAPSLRKCPICRAKIKGTVRTFLS 54
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
254-324 7.59e-33

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


Pssm-ID: 197595  Cd Length: 71  Bit Score: 120.11  E-value: 7.59e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 163644309   254 THAARIRTFSNWPSSALVHSQELASAGFYYTGHSDDVKCFCCDGGLRCWESGDDPWVEHAKWFPRCEYLLR 324
Cdd:smart00238   1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVRN 71
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
256-323 7.10e-32

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 117.37  E-value: 7.10e-32
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163644309 256 AARIRTFSNWPSSALVHSQELASAGFYYTGHSDDVKCFCCDGGLRCWESGDDPWVEHAKWFPRCEYLL 323
Cdd:cd00022    1 EARLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVL 68
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
258-323 6.08e-30

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteristically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 334196  Cd Length: 69  Bit Score: 112.00  E-value: 6.08e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644309  258 RIRTF-SNWPSSAL--VHSQELASAGFYYTGHSDDVKCFCCDGGLRCWESGDDPWVEHAKWFPRCEYLL 323
Cdd:pfam00653   1 RLATFkDNWPLSAKspPSPEELAEAGFYYTGTGDRVQCFYCGGELDGWEPGDDPWEEHKKHSPNCPFLK 69
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
168-236 1.07e-29

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


Pssm-ID: 197595  Cd Length: 71  Bit Score: 111.26  E-value: 1.07e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644309   168 TEKARLLTYETWP-LSFLSPAKLAKAGFYYIGPGDRVACFACDGKLSNWERKDDAMSEHQRHFPSCPFLK 236
Cdd:smart00238   1 SEEARLKTFQNWPyNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVR 70
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
170-236 3.37e-29

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 110.05  E-value: 3.37e-29
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163644309 170 KARLLTYETWPLS-FLSPAKLAKAGFYYIGPGDRVACFACDGKLSNWERKDDAMSEHQRHFPSCPFLK 236
Cdd:cd00022    1 EARLKTFKNWPISlKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVL 68
BIR smart00238
Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis ...
28-97 8.86e-29

Baculoviral inhibition of apoptosis protein repeat; Domain found in inhibitor of apoptosis proteins (IAPs) and other proteins. Acts as a direct inhibitor of caspase enzymes.


Pssm-ID: 197595  Cd Length: 71  Bit Score: 108.94  E-value: 8.86e-29
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644309    28 CELYRLSTYSAFPRGVPVSERSLARAGFYYTGANDKVKCFCCGLMLDNWKQGDSPMEKHRKLYPSCNFVQ 97
Cdd:smart00238   1 SEEARLKTFQNWPYNSKCTPEQLAEAGFYYTGVGDEVKCFFCGGELDNWEPGDDPWEEHKKWSPNCPFVR 70
BIR cd00022
Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis ...
32-97 2.49e-28

Baculoviral inhibition of apoptosis protein repeat domain; Found in inhibitors of apoptosis proteins (IAPs) and other proteins. In higher eukaryotes, BIR domains inhibit apoptosis by acting as direct inhibitors of the caspase family of protease enzymes. In yeast, BIR domains are involved in regulating cytokinesis. This novel fold is stabilized by zinc tetrahedrally coordinated by one histidine and three cysteine residues and resembles a classical zinc finger.


Pssm-ID: 237989  Cd Length: 69  Bit Score: 107.35  E-value: 2.49e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 163644309  32 RLSTYSAFPRGVPVSERSLARAGFYYTGANDKVKCFCCGLMLDNWKQGDSPMEKHRKLYPSCNFVQ 97
Cdd:cd00022    3 RLKTFKNWPISLKVTPEKLAEAGFYYTGRGDEVKCFFCGLELKNWEPGDDPWEEHKRWSPNCPFVL 68
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
172-236 1.76e-26

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteristically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 334196  Cd Length: 69  Bit Score: 102.37  E-value: 1.76e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644309  172 RLLTY-ETWPLSFL---SPAKLAKAGFYYIGPGDRVACFACDGKLSNWERKDDAMSEHQRHFPSCPFLK 236
Cdd:pfam00653   1 RLATFkDNWPLSAKsppSPEELAEAGFYYTGTGDRVQCFYCGGELDGWEPGDDPWEEHKKHSPNCPFLK 69
BIR pfam00653
Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein ...
32-97 2.73e-26

Inhibitor of Apoptosis domain; BIR stands for 'Baculovirus Inhibitor of apoptosis protein Repeat'. It is found repeated in inhibitor of apoptosis proteins (IAPs), and in fact it is also known as IAP repeat. These domains characteristically have a number of invariant residues, including 3 conserved cysteines and one conserved histidine that coordinate a zinc ion. They are usually made up of 4-5 alpha helices and a three-stranded beta-sheet. BIR is also found in other proteins known as BIR-domain-containing proteins (BIRPs), such as Survivin.


Pssm-ID: 334196  Cd Length: 69  Bit Score: 101.60  E-value: 2.73e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 163644309   32 RLSTY-SAFPRG--VPVSERSLARAGFYYTGANDKVKCFCCGLMLDNWKQGDSPMEKHRKLYPSCNFVQ 97
Cdd:pfam00653   1 RLATFkDNWPLSakSPPSPEELAEAGFYYTGTGDRVQCFYCGGELDGWEPGDDPWEEHKKHSPNCPFLK 69
RING-HC_BIRC4_8 cd16714
RING finger, HC subclass, found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP ...
543-602 4.14e-25

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) pathway, the nuclear factor-kappaB (NF-kappaB) pathway, and the transforming growth factor-beta (TGF-beta) pathway. Moreover, XIAP can regulate copper homeostasis through 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: 319628  Cd Length: 62  Bit Score: 98.34  E-value: 4.14e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644309 543 EEQLRKLQEERMCKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICRGTIKGTVRTFLS 602
Cdd:cd16714    3 EEQLRRLQEEKLCKICMDRNIAIVFIPCGHLVTCKQCAEALDKCPICCTVITFKQKIFMS 62
UBA_BIRC2_3 cd14394
UBA domain found in baculoviral IAP repeat-containing protein BIRC2, BIRC3 and similar ...
376-425 4.70e-23

UBA domain found in baculoviral IAP repeat-containing protein BIRC2, BIRC3 and similar proteins; The subfamily includes cellular inhibitor of apoptosis protein 1 (c-IAP1) and c-IAP2. c-IAPs function as ubiquitin E3 ligases that mediate the ubiquitination of the substrates involved in apoptosis, nuclear factor-kappaB (NF-kappaB)signaling, and oncogenesis. Unlike other apoptosis proteins (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 called 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 called 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 binds polyubiquitin (polyUb), a caspase activation and recruitment domain (CARD) that serves as a protein interaction surface, and a RING domain at the carboxyl terminus that is required for ubiquitin ligase activity.


Pssm-ID: 270577  Cd Length: 50  Bit Score: 91.90  E-value: 4.70e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 163644309 376 MSTPVVKAALEMGFSRSLVRQTVQWQILATGENYRTVSDLVIGLLDAEDE 425
Cdd:cd14394    1 MNTPVVKSALEMGFNRRLVKQTVQSKILTSGENYKTVNDLVSDLLSAEDE 50
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
443-526 6.34e-22

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 334175  Cd Length: 85  Bit Score: 89.92  E-value: 6.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644309  443 LALIRKNKMVLFQHLTCVTPMLYCLLSARAITEQECNAVKQKPHTL-QASTLIDTVLAKGNTAATSFRNSLREIDPALYR 521
Cdd:pfam00619   1 LELLKKNREALVERLTTLDGLLDYLLEKNVLTEEEYEKIKANTTRLdKARELLDLVLKKGPEACQIFLQALKEGDPDLAS 80

                  ....*
gi 163644309  522 DIFVQ 526
Cdd:pfam00619  81 LLELL 85
RING-HC_IAPs cd16510
RING finger, HC subclass, found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently ...
552-590 9.29e-19

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 binds 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 UBA and C3HC4-type RING-HC domains. CARD domain may serve as a protein interaction surface.


Pssm-ID: 319424  Cd Length: 39  Bit Score: 79.47  E-value: 9.29e-19
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 163644309 552 ERMCKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICR 590
Cdd:cd16510    1 ERLCKICMDREVSIVFVPCGHLVVCEECAPALDKCPICR 39
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
551-594 1.05e-15

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 339001 [Multi-domain]  Cd Length: 48  Bit Score: 70.87  E-value: 1.05e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 163644309  551 EERMCKVCMDREVSIVFIPCGHLVVCKDCAPSLR----KCPICRGTIK 594
Cdd:pfam13920   1 EDRLCVICLDRPRNVVLLPCGHLCLCEECAERLRkkkkKCPICRQPIE 48
RING-HC_CblA_like cd16501
RING finger, HC subclass, found in Dictyostelium discoideum Cbl-like protein A (CblA) and ...
554-590 3.15e-12

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 kinases 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: 319415  Cd Length: 37  Bit Score: 60.96  E-value: 3.15e-12
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 163644309 554 MCKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICR 590
Cdd:cd16501    1 LCKVCMDNEINTVFLPCGHVICCSECAARLSKCPICR 37
RING-HC_LRSAM1 cd16515
RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing ...
555-593 9.79e-12

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: 319429  Cd Length: 40  Bit Score: 59.61  E-value: 9.79e-12
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 163644309 555 CKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICRGTI 593
Cdd:cd16515    2 CVICLEQESQMIFLPCGHVCCCQTCSAPLQSCPLCRGDI 40
UBA_IAPs cd14321
UBA domain found in inhibitor of apoptosis proteins (IAPs); IAPs are frequently overexpressed ...
379-422 1.09e-11

UBA domain 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 and c-IAP2, XIAP, 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 binds polyubiquitin (polyUb), and a RING domain at the carboxyl terminus that is required for ubiquitin ligase activity. c-IAPs contains an additional caspase activation and recruitment domain (CARD) between UBA and RING domains. CARD domain may serve as a protein interaction surface.


Pssm-ID: 270506  Cd Length: 44  Bit Score: 59.36  E-value: 1.09e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 163644309 379 PVVKAALEMGFSRSLVRQTVQWQILATGENYRTVSDLVIGLLDA 422
Cdd:cd14321    1 PVVQSALEMGFDRDRVRRAIERRLEETGRPFSTAEELVEAVLNA 44
RING-HC_CARP cd16500
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, ...
554-590 2.55e-10

RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein CARP-1, CARP-2 and similar proteins; The CARPs family 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 enhancing 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: 319414  Cd Length: 39  Bit Score: 55.53  E-value: 2.55e-10
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 163644309 554 MCKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICR 590
Cdd:cd16500    1 LCKICMDAPIDCVLLECGHMVTCTKCGKRMSECPICR 37
mRING-HC-C3HC5_CGRF1 cd16787
Modified RING finger, HC subclass (C3HC5-type), found in cell growth regulator with RING ...
555-590 7.20e-10

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 of tissue 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: 319701  Cd Length: 37  Bit Score: 54.24  E-value: 7.20e-10
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 163644309 555 CKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICR 590
Cdd:cd16787    2 CVVCQNAPINRVLLPCRHACLCSGCFKKLKRCPMCR 37
RING-HC_MIBs_like cd16520
RING finger, HC subclass, found in mind bomb MIB1, MIB2, RGLG1, RGLG2, and similar proteins; ...
554-593 3.13e-09

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 family 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, RING domain ligase RGLG1, RGLG2 and similar proteins from plant have also been included in this family. 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: 319434  Cd Length: 38  Bit Score: 52.39  E-value: 3.13e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 163644309 554 MCKVCMDREVSIVFIpCGHlVVCKDCAPSLRKCPICRGTI 593
Cdd:cd16520    1 LCPICMDRKRNVAFL-CGH-GACQKCGEPLKECPICRKPI 38
RING-HC_CARP1 cd16706
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 1 (CARP1) ...
554-590 1.17e-08

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 the 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: 319620  Cd Length: 39  Bit Score: 50.70  E-value: 1.17e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 163644309 554 MCKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICR 590
Cdd:cd16706    1 LCRICMDAVIDCVLLECGHMVTCTKCGKRMSECPICR 37
RING-HC_MYLIP cd16523
RING finger, HC subclass, found in myosin regulatory light chain interacting protein (MYLIP) ...
554-590 2.28e-08

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: 319437  Cd Length: 38  Bit Score: 49.82  E-value: 2.28e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 163644309 554 MCKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICR 590
Cdd:cd16523    1 LCMVCCEEEINSAFCPCGHMVCCESCAAQLQSCPVCR 37
RING2-HC_MIB1 cd16725
RING finger 2, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known ...
555-590 3.07e-08

RING finger 2, 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 consisted of three C3HC4-type RING-HC fingers. This family corresponds to the second RING-HC finger.


Pssm-ID: 319639  Cd Length: 37  Bit Score: 49.37  E-value: 3.07e-08
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 163644309 555 CKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICR 590
Cdd:cd16725    2 CVVCSDKKASVLFKPCGHMCACEGCASLMKKCVQCR 37
mRING-HC-C3HC5_MAPL cd16648
Modified RING finger, HC subclass (C3HC5-type), found in mitochondrial-anchored protein ligase ...
555-590 3.63e-08

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: 319562  Cd Length: 40  Bit Score: 49.33  E-value: 3.63e-08
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 163644309 555 CKVCMDREVSIVFIPCGHLVVCKDCA---PSLRKCPICR 590
Cdd:cd16648    2 CVICLSNPRSCVLLECGHVCSCIECAralPSPKQCPICR 40
RING-HC_MIBs cd16519
RING finger, HC subclass, found in mind bomb MIB1, MIB2, and similar proteins; MIBs are large, ...
555-590 7.44e-08

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 family corresponds to the first RING-HC finger of MIB1 and MIB2, as well as the second RING-HC finger of MIB1.


Pssm-ID: 319433  Cd Length: 37  Bit Score: 48.30  E-value: 7.44e-08
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 163644309 555 CKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICR 590
Cdd:cd16519    2 CRVCSDPANLVLFQPCGHVVACEDCSLRVKKCLQCK 37
mRING-HC-C3HC5_MGRN1_like---blasttree cd16789
Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 ...
555-590 1.09e-07

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


Pssm-ID: 319703  Cd Length: 41  Bit Score: 48.11  E-value: 1.09e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 163644309 555 CKVCMDREVSIVFIPCGHLVVCKDCAPSLR----KCPICR 590
Cdd:cd16789    2 CVICLSDPRDTTVLPCRHLCLCSECAEVLRyqsnKCPICR 41
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
440-520 1.52e-07

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain.


Pssm-ID: 128424  Cd Length: 88  Bit Score: 49.26  E-value: 1.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644309   440 SDDLALIRKNKMVLFQHLTCVtPMLYCLLSARAITEQECNAVKQKPHTL-QASTLIDTVLAKGNTAATSFRNSLREIDPA 518
Cdd:smart00114   3 ERDKRLLRRNRVRLGEELGVD-GLLDYLVEKNVLTEKEIEAIKAATTKLrDKRELVDSLQKRGSQAFDTFLDSLQETDQK 81

                   ..
gi 163644309   519 LY 520
Cdd:smart00114  82 LA 83
RING-HC_UNK cd16771
RING finger, HC subclass, found in RING finger protein unkempt (UNK) and similar proteins; UNK, ...
555-589 1.60e-07

RING finger, HC subclass, found in RING finger protein unkempt (UNK) 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 the 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. UNK contains six tandem CCCH-type zinc fingers at the N-terminus, and a C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 319685  Cd Length: 37  Bit Score: 47.48  E-value: 1.60e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 163644309 555 CKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPIC 589
Cdd:cd16771    2 CMKCQERNRSVTVLPCQHLVLCETCAEAVTECPYC 36
RING-HC_RSPRY1 cd16566
RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) ...
554-593 2.12e-07

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: 319480 [Multi-domain]  Cd Length: 41  Bit Score: 47.35  E-value: 2.12e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 163644309 554 MCKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICRGTI 593
Cdd:cd16566    2 CCTLCFDKVADTTLRPCGHSGFCMDCALQLETCPLCRQPI 41
UBA_XtBIRC7_like cd14396
UBA domain found in Xenopus tropicalis baculoviral IAP repeat-containing protein BIRC7, ...
379-422 2.19e-07

UBA domain found in Xenopus tropicalis baculoviral IAP repeat-containing protein BIRC7, BIRC71A and similar proteins; X. tropicalis BIRC7, also called E3 ubiquitin-protein ligase EIAP, embryonic/Egg IAP (xEIAP/XLX), inhibitor of apoptosis (IAP)-like protein, XIAP homolog XLX, is a weak apoptosis inhibitor that exhibits caspase inhibition and autoubiquitylation. It is uniquely modified by MAPK- and Cdc2/Cyclin B-dependent phosphorylation during oocyte maturation. Its caspase-dependent cleavage is altered when it is phosphorylated. X. tropicalis BIRC7 contains two N-terminal baculoviral IAP repeats (BIRs) and a C-terminal RING domain. Based on sequence homology, it also harbors a ubiquitin-associated (UBA) domain which is not detected in human BIRC7.


Pssm-ID: 270579  Cd Length: 44  Bit Score: 47.39  E-value: 2.19e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 163644309 379 PVVKAALEMGFSRSLVRQTVQWQILATGENYRTVSDLVIGLLDA 422
Cdd:cd14396    1 SVVQAVLQMGFDQSLVESLVQNKYLLTGPAYTSVSQLVSDLLQE 44
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
446-523 2.27e-07

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260018  Cd Length: 79  Bit Score: 48.28  E-value: 2.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 163644309 446 IRKNKMVLFQHLtCVTPMLYCLLSARAITEQECNAVKQKPH-TLQASTLIDTVLAKGNTAATSFRNSLREID-PALYRDI 523
Cdd:cd01671    1 LRKNRVELVEDL-DVEDILDHLIQKGVLTEEDKEEILSEKTrQDKARKLLDILPRRGPKAFEVFCEALRETGqPHLAELL 79
RING-HC_CARP2 cd16707
RING finger, HC subclass, found in caspases-8 and -10-associated RING finger protein 2 (CARP-2) ...
554-590 6.28e-07

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 through degrading 14-3-3 sigma 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: 319621  Cd Length: 40  Bit Score: 45.75  E-value: 6.28e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 163644309 554 MCKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICR 590
Cdd:cd16707    2 LCKICMDSPIDCVLLECGHMVTCTKCGKRMSECPICR 38
RING1-HC_MIB1 cd16724
RING finger 1, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known ...
555-590 7.20e-07

RING finger 1, 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 consisted of three C3HC4-type RING-HC fingers. This family corresponds to the first RING-HC finger.


Pssm-ID: 319638  Cd Length: 37  Bit Score: 45.50  E-value: 7.20e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 163644309 555 CKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICR 590
Cdd:cd16724    2 CMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLLCK 37
RING2-HC_MIB2 cd16728
RING finger 2, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also known ...
554-601 8.63e-07

RING finger 2, 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 consisted of two C3HC4-type RING-HC fingers. This family corresponds to the second RING-HC finger.


Pssm-ID: 319642  Cd Length: 46  Bit Score: 45.60  E-value: 8.63e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 163644309 554 MCKVCMDREVSIVFiPCGHlVVCKDCAPSLRKCPICRGTIKGTVRTFL 601
Cdd:cd16728    1 TCPICIDNHIKLVF-QCGH-GSCIECSSALKACPICRQAIRERIQIFV 46
RING-HC_UNKL cd16772
RING finger, HC subclass, found in RING finger protein unkempt-like (UNKL) and similar ...
553-590 1.18e-06

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: 319686  Cd Length: 38  Bit Score: 45.24  E-value: 1.18e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 163644309 553 RMCKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPICR 590
Cdd:cd16772    1 KKCIVCQERDRSIVLQPCQHYVLCEPCAATKPECPYCK 38
UBA_BIRC4_8 cd14395
UBA domain found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP repeat-containing ...
375-423 1.27e-06

UBA domain found in E3 ubiquitin-protein ligase XIAP, baculoviral IAP repeat-containing protein 8 (BIRC8) and similar proteins; XIAP, also called 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) pathway, the nuclear factor-kappaB (NF-kappaB) pathway, and the transforming growth factor-beta (TGF-beta) pathway. Moreover, XIAP can regulate copper homeostasis through interacting with MURR1. BIRC8, also called inhibitor of apoptosis-like protein 2 (IAP-like protein 2 or 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 RING domain at the carboxyl terminus.


Pssm-ID: 270578  Cd Length: 50  Bit Score: 45.21  E-value: 1.27e-06
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gi 163644309 375 MMSTPVVKAALEMGFSRSLVRQTVQWQILATGENYRTVSDLVIGLLDAE 423
Cdd:cd14395    1 ILQNPLVQEAIRMGFSFKEIKKIMEEKLKTSGSNYTSLEVLVADLVSAQ 49
mRING-HC-C3HC5_NEU1B cd16786
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1B (NEURL1B); ...
555-590 1.44e-06

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: 319700  Cd Length: 43  Bit Score: 44.91  E-value: 1.44e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 163644309 555 CKVCMDREVSIVFIPCGHLVVCKDCAPSLRK-----CPICR 590
Cdd:cd16786    2 CTVCFDNEVDTVIYTCGHMCLCNSCGLKLKRqinacCPICR 42
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; RING finger is a specialized type of ...
555-589 2.55e-06

HC subclass of RING (RING-HC) finger and its variants; 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 HC subclass of RING (RING-HC) finger proteins 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 finger 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: 319363 [Multi-domain]  Cd Length: 39  Bit Score: 44.00  E-value: 2.55e-06
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gi 163644309 555 CKVCMDREVSIVFIPCGHlVVCKDCAPSLRK-----CPIC 589
Cdd:cd16449    1 CPICLELLKDPVLLPCGH-TFCRSCLRRLLKegkkkCPIC 39
mRING-HC-C3HC5_NEU1 cd16647
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, ...
555-590 3.69e-06

Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, NEURL1B, and similar proteins; The family 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 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. Members in this family 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: 319561  Cd Length: 42  Bit Score: 43.83  E-value: 3.69e-06
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gi 163644309 555 CKVCMDREVSIVFIPCGHLVVCKDCAPSLRK-----CPICR 590
Cdd:cd16647    2 CTVCYDRPVDSVLYRCGHMCMCYECALRLKRqsggsCPICR 42
RING1-HC_MIB2 cd16726
RING finger 1, HC subclass, found in mind bomb 2 (MIB2) and similar proteins; MIB2, also known ...
555-589 3.96e-06

RING finger 1, 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 consisted of two C3HC4-type RING-HC fingers. This family corresponds to the first RING-HC finger.


Pssm-ID: 319640  Cd Length: 37  Bit Score: 43.64  E-value: 3.96e-06
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gi 163644309 555 CKVCMDREVSIVFIPCGHLVVCKDCAPSLRKCPIC 589
Cdd:cd16726    2 CIVCSELAALVTFEPCQHSIVCEECARRMKKCIKC 36
RING3-HC_MIB1 cd16727
RING finger 3, HC subclass, found in mind bomb 1 (MIB1) and similar proteins; MIB1, also known ...
554-593 2.38e-05

RING finger 3, 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 consisted of three C3HC4-type RING-HC fingers. This family corresponds to the third RING-HC finger.


Pssm-ID: 319641  Cd Length: 42  Bit Score: 41.67  E-value: 2.38e-05
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gi 163644309 554 MCKVCMDREVSIVFIpCGHlVVCKDCAPSLRKCPICRGTI 593
Cdd:cd16727    1 MCPVCLDRLKNMIFL-CGH-GTCQLCGDRMSECPICRKAV 38
mRING-HC-C2H2C4_MDM2_like cd16646
Modified RING finger, HC subclass (C2H2C4-type), found in E3 ubiquitin-protein ligase MDM2, ...
555-590 4.98e-05

Modified RING finger, HC subclass (C2H2C4-type), found in E3 ubiquitin-protein ligase MDM2, protein MDM4 and similar proteins; MDM2 (also known as HDM2) and MDM4 (also known as MDMX or HDMX) are the primary p53 tumor suppressor negative regulators. They have non-redundant roles in the regulation of p53. MDM2 mainly functions to control p53 stability, while MDM4 controls p53 transcriptional activity. Both MDM2 and MDM4 contain an N-terminal p53-binding domain, a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region, and a C-terminal modified C2H2C4-type RING-HC finger. Mdm2 can form homo-oligomers through its RING domain and displays E3 ubiquitin ligase activity that catalyzes the attachment of ubiquitin to p53 as an essential step in the regulation of its level in cells. Despite its RING domain and structural similarity with MDM2, MDM4 does not homo-oligomerize and lacks ubiquitin-ligase function, but inhibits the transcriptional activity of p53. In addition, both their RING domains are responsible for the hetero-oligomerization, which is crucial for the suppression of P53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. Moreover, MDM2 and MDM4 can be phosphorylated and destabilized in response to DNA damage stress. In response to ribosomal stress, MDM2-mediated p53 ubiquitination and degradation can be inhibited through the interaction with ribosomal proteins L5, L11, and L23. However, MDM4 is not bound to ribosomal proteins, suggesting its different response to regulation by small basic proteins such as ribosomal proteins and ARF.


Pssm-ID: 319560  Cd Length: 44  Bit Score: 40.78  E-value: 4.98e-05
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gi 163644309 555 CKVCMD--REVSIVFIPCGHLVVCKDCAPSLRK----CPICR 590
Cdd:cd16646    1 CVICLSrpRTASIVHGKTGHQVCCYTCAKKLKRrgkpCPVCR 42
RING-HC_Cbl_like cd16502
RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor ...
554-590 5.90e-05

RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor proteins family contains a small class of RING-type E3 ubiquitin ligases with oncogenic activity, which is represented by three mammalian members, c-Cbl, Cbl-b and Cbl-c, as well as two invertebrate Cbl-family proteins, D-Cbl in Drosophila and Sli-1 in C. elegans. Cbl proteins function as potent negative regulators of various signaling cascades in a wide range of cell types. They play roles in ubiquitinating the activated tyrosine kinases and targeting them for degradation. D-Cbl associates with the Drosophila epidermal growth factor receptor (EGFR) and overexpression of D-Cbl in the eye of Drosophila embryos inhibits EGFR dependent photoreceptor cell development. Sli-1 is a negative regulator of the Let-23 receptor tyrosine kinase, an EGFR homolog, in vulva development. Cbl proteins in this family consist of a highly conserved N-terminal half that includes a tyrosine-kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain) and a C3HC4-type RING-HC finger, both of which are required for Cbl-mediated downregulation of RTKs, and a divergent C-terminal region.


Pssm-ID: 319416 [Multi-domain]  Cd Length: 43  Bit Score: 40.42  E-value: 5.90e-05
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gi 163644309 554 MCKVCMDREVSIVFIPCGHLvVCKDCAPSLRK-----CPICR 590
Cdd:cd16502    3 LCKICAENDKDVRIEPCGHL-LCTPCLTSWQDsdgqtCPFCR 43
RING-HC_RGLG_plant cd16729
RING finger, HC subclass, found in RING domain ligase RGLG1, RGLG2 and similar proteins from ...
554-600 1.01e-04

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. All members in this family contain a Von Willebrand factor type A (vWA) domain and a C3HC4-type RING-HC finger.


Pssm-ID: 319643  Cd Length: 45  Bit Score: 39.73  E-value: 1.01e-04
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gi 163644309 554 MCKVCMDREVSIVFiPCGHLVvCKDCAPSLRKCPICRGTIKGTVRTF 600
Cdd:cd16729    1 LCPICLSNRKDLAF-GCGHQT-CCECGQSLTACPICRQPITTRIRLY 45
mRING-HC-C3HC5_RNF26 cd16788
Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 26 (RNF26) and ...
553-593 1.42e-04

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


Pssm-ID: 319702  Cd Length: 48  Bit Score: 39.34  E-value: 1.42e-04
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gi 163644309 553 RMCKVCMDREVSIVFIPCGHLVVCKDCAPSL-------RKCPICRGTI 593
Cdd:cd16788    1 KKCVICQDQVKTVLLLPCRHMCLCRGCANILlrqpvyqRNCPLCRSMI 48
RING-HC_MEX3B cd16721
RING finger, HC subclass, found in RNA-binding protein MEX3B; MEX3B, also known as RING finger ...
553-590 1.52e-04

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 a 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: 319635  Cd Length: 43  Bit Score: 39.10  E-value: 1.52e-04
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gi 163644309 553 RMCKVCMDREVSIVFIPCGHLVVCKDCAPSL-----RKCPICR 590
Cdd:cd16721    1 RDCSVCFESEVIAALVPCGHNLFCMECANRIceksePECPVCH 43
mRING-HC-C3HC5_CGRF1_like cd16649
Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 ...
555-590 1.66e-04

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


Pssm-ID: 319563  Cd Length: 41  Bit Score: 39.08  E-value: 1.66e-04
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gi 163644309 555 CKVCMDREVSIVFIPCGHLVVCKDCAPSLRK----CPICR 590
Cdd:cd16649    2 CVVCQNGTVNWLLLPCRHLCLCDGCVKYLQYqannCPMCR 41
Prok-RING_4 pfam14447
Prokaryotic RING finger family 4; RING finger family domain found sporadically in bacteria. ...
555-590 1.84e-04

Prokaryotic RING finger family 4; RING finger family domain found sporadically in bacteria. The finger is fused to an N-terminal alpha-helical domain, ROT/Trove-like repeats and a C-terminal TerD domain. The architecture suggests a possible role in an RNA-processing complex.


Pssm-ID: 316929  Cd Length: 46  Bit Score: 39.27  E-value: 1.84e-04
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gi 163644309  555 CKVCMDREVSIVFIPCGHLvVCKDCAPS--LRKCPICR 590
Cdd:pfam14447   1 CVLCGRVGTVHILSPCGHL-VCRDCFDGsdYSGCPICH 37
RING-HC_MEX3A cd16720
RING finger, HC subclass, found in RNA-binding protein MEX3A; MEX3A, also known as RING finger ...
553-589 2.09e-04

RING finger, HC subclass, found in RNA-binding protein MEX3A; MEX3A, also known as RING finger and KH domain-containing protein 4 (RKHD4), is a RNA-binding phosphoprotein that localizes in P-bodies and stress granules, which are two structures involved in the storage and turnover of mRNAs. It has been implicated in the regulation of tumorigenesis. It controls the polarity and stemness of intestinal epithelial cells through the post-transcriptional regulation of the homeobox transcription factor CDX2, which plays a crucial role in intestinal cell fate specification, both during normal development and in tumorigenic processes involving intestinal reprogramming. Moreover, it exhibits a transforming activity when overexpressed in gastric epithelial cells. MEX3A 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, MEX3A shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway.


Pssm-ID: 319634  Cd Length: 43  Bit Score: 38.72  E-value: 2.09e-04
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gi 163644309 553 RMCKVCMDREVSIVFIPCGHLVVCKDCAPSL-----RKCPIC 589
Cdd:cd16720    1 RDCMVCFESEVTAALVPCGHNLFCMECAVRIcernePECPVC 42
RING-HC_MEX3D cd16723
RING finger, HC subclass, found in RNA-binding protein MEX3D; MEX3D, also known as RING finger ...
553-590 2.62e-04

RING finger, HC subclass, found in RNA-binding protein MEX3D; MEX3D, also known as RING finger and KH domain-containing protein 1 (RKHD1), RING finger protein 193 (RNF193), or TINO, is a RNA-binding phosphoprotein that controls the stability of the transcripts coding for the anti-apoptotic protein BCL-2, and negatively regulates BCL-2 in HeLa cells. MEX3D 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, MEX3D shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway.


Pssm-ID: 319637  Cd Length: 45  Bit Score: 38.72  E-value: 2.62e-04
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gi 163644309 553 RMCKVCMDREVSIVFIPCGHLVVCKDCA-----PSLRKCPICR 590
Cdd:cd16723    1 RDCVVCFESEVIAALVPCGHNLFCMECAiriceKSEPECPACH 43
mRING-HC-C2H2C4_MDM4 cd16784
Modified RING finger, HC subclass (C2H2C4-type), found in protein MDM4 and similar proteins; ...
555-602 2.68e-04

Modified RING finger, HC subclass (C2H2C4-type), found in protein MDM4 and similar proteins; MDM4, also known as double minute 4 protein (Hdm4), or MDM2-like p53-binding protein, or protein MDMX, or HDMX, or p53-binding protein MDM4, exerts its oncogenic activity predominantly by binding p53 tumor suppressor and blocking its transcriptional activity. MDM4 is phosphorylated and destabilized in response to DNA damage stress. It can also be specifically dephosphorylated through directly interacting with protein phosphatase 1 (PP1), which may increase its stability and thus inhibits p53 activity. Meanwhile, MDM4 has a p53-independent role in tumorigenesis and cell growth regulation. MDM4 contains an N-terminal p53-binding domain and a C-terminal modified C2H2C4-type RING-HC finger responsible for its hetero-oligomerization, which is crucial for the suppression of P53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. MDM4 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region.


Pssm-ID: 319698  Cd Length: 59  Bit Score: 39.00  E-value: 2.68e-04
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gi 163644309 555 CKVCM--DREVSIVFIPCGHLVVCKDCAPSLRK----CPICRGTIKGTVRTFLS 602
Cdd:cd16784    6 CSLCQkrPRNGNIVHGRTAHLVTCFHCARMLKKagapCPVCKKQIQMVIKIFIA 59
RING-HC_MEX3 cd16518
RING finger, HC subclass, found in RNA-binding proteins of the evolutionarily-conserved MEX-3 ...
555-590 2.98e-04

RING finger, HC subclass, found in RNA-binding proteins of the evolutionarily-conserved MEX-3 family; The family includes MEX-3 family phosphoproteins have been found in vertebrates. They are mediators of post-transcriptional regulation in different organisms, and have been implicated in many core biological processes, including embryonic development, epithelial homeostasis, immune responses, metabolism, and cancer. They contain two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. They shuttle between the nucleus and the cytoplasm via the CRM1-dependent export pathway. The RNA-binding protein MEX-3 from nematode Caenorhabditis elegans is the founding member of the MEX-3 family. Due to the lack of RING-HC finger, it is not included here.


Pssm-ID: 319432  Cd Length: 41  Bit Score: 38.50  E-value: 2.98e-04
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gi 163644309 555 CKVCMDREVSIVFIPCGHLVVCKDCAPSL-----RKCPICR 590
Cdd:cd16518    1 CVVCFESEVVAALVPCGHNLFCMECANRIceksdAECPVCH 41
RING-HC_Cbl cd16708
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl and similar proteins; Cbl, ...
553-596 3.55e-04

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl and similar proteins; Cbl, also known as Casitas B-lineage lymphoma proto-oncogene, proto-oncogene c-Cbl, RING finger protein 55 (RNF55), or signal transduction protein Cbl, is a multi-domain protein that acts as a key negative regulator of various receptor and non-receptor tyrosine kinases signaling. It contains a tyrosine kinase-binding domaina (TKB, also known as the phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain), a proline-rich domain, a C3HC4-type RING-HC finger, and an ubiquitin-associated (UBA) domain. TKB is responsible for the interactions with many tyrosine kinases, such as the colony-stimulating factor-1 (CSF-1) receptor, Syk/ZAP-70, and Src-family of protein tyrosine kinases. The proline-rich domain can recruit proteins with a SH3 domain. Moreover, Cbl functions as an E3 ubiquitin ligase that can bind ubiquitin-conjugating enzymes (E2s) through the RING-HC finger.


Pssm-ID: 319622  Cd Length: 57  Bit Score: 38.49  E-value: 3.55e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 163644309 553 RMCKVCMDREVSIVFIPCGHLvVCKDCAPSLRK-----CPICRGTIKGT 596
Cdd:cd16708    2 QLCKICAENDKDVKIEPCGHL-MCTSCLTSWQEsegqgCPFCRCEIKGT 49
RING-HC_Cbl-b cd16709
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-b and similar proteins; ...
553-596 6.43e-04

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-b and similar proteins; Cbl-b, also known as Casitas B-lineage lymphoma proto-oncogene b, RING finger protein 56 (RNF56), SH3-binding protein Cbl-b, or signal transduction protein Cbl-b, has been identified as a regulator of antigen-specific, T cell-intrinsic, peripheral immune tolerance, a state also known as clonal anergy. It may inhibit activation of the p85 subunit of phosphoinositide 3-kinase (PI3K), protein kinase C-theta (PKC-theta), and phospholipase C-gamma1 (PLC-gamma1) and negatively regulates T-cell receptor-induced transcription factor nuclear factor kappaB (NF-kappaB) activation. In addition, Cbl-b may target multiple signaling molecules involved in transforming growth factor (TGF)-beta-mediated transactivation pathways. Cbl-b contains a tyrosine-kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain), a proline rich domain, a nuclear localization signal, a C3HC4-type RING-HC finger and an ubiquitin-associated (UBA) domain.


Pssm-ID: 319623  Cd Length: 66  Bit Score: 38.15  E-value: 6.43e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 163644309 553 RMCKVCMDREVSIVFIPCGHLvVCKDCAPSLRK-----CPICRGTIKGT 596
Cdd:cd16709   18 QLCKICAENDKDVKIEPCGHL-MCTSCLTAWQEsdgqgCPFCRCEIKGT 65
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
555-589 2.03e-03

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 35.95  E-value: 2.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 163644309   555 CKVCMDR-EVSIVFIPCGHlVVCKDCAPSL-----RKCPIC 589
Cdd:smart00184   1 CPICLEEyLKDPVILPCGH-TFCRSCIRKWlesgnNTCPIC 40
mRING-HC-C2H2C4_MDM2 cd16783
Modified RING finger, HC subclass (C2H2C4-type), found in E3 ubiquitin-protein ligase MDM2 and ...
555-602 2.29e-03

Modified RING finger, HC subclass (C2H2C4-type), found in E3 ubiquitin-protein ligase MDM2 and similar proteins; MDM2, also known as double minute 2 protein (Hdm2), oncoprotein MDM2, or p53-binding protein, exerts its oncogenic activity predominantly by binding p53 tumor suppressor and blocking its transcriptional activity. It forms homo-oligomers and displays E3 ubiquitin ligase activity that catalyzes the attachment of ubiquitin to p53 as an essential step in the regulation of its level in cells. Moreover, in response to ribosomal stress, MDM2-mediated p53 ubiquitination and degradation can be inhibited through its interaction with ribosomal proteins L5, L11, and L23. MDM2 can be phosphorylated in the DNA damage. Meanwhile, MDM2 has a p53-independent role in tumorigenesis and cell growth regulation. In addition, it binds interferon (IFN) regulatory factor-2 (IRF-2), an IFN-regulated transcription factor, and mediates its ubiquitination. MDM2 contains an N-terminal p53-binding domain, and a C-terminal modified C2H2C4-type RING-HC finger conferring E3 ligase activity that is required for ubiquitination and nuclear export of p53. It is also responsible for the hetero-oligomerization of MDM2, which is crucial for the suppression of P53 activity during embryonic development, and the recruitment of E2 ubiquitin-conjugating enzymes. MDM2 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain, as well as a nuclear localization signal (NLS) and a nuclear export signal (NES), near the central acidic region. The zf-RanBP2 domain plays an important role in mediating MDM2 binding to ribosomal proteins and thus is involved in MDM2-mediated p53 suppression.


Pssm-ID: 319697  Cd Length: 57  Bit Score: 36.44  E-value: 2.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 163644309 555 CKVCMDREVS--IVFIPCGHLVVCKDCAPSLRK----CPICRGTIKGTVRTFLS 602
Cdd:cd16783    4 CVICQGRPKNgcIVHGKTGHLMACFTCAKKLKKrnkpCPVCRQPIQMIVLTYFS 57
mRING-HC-C3HC5_NEU1A cd16785
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1A (NEURL1A) ...
555-590 2.50e-03

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


Pssm-ID: 319699  Cd Length: 44  Bit Score: 36.02  E-value: 2.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 163644309 555 CKVCMDREVSIVFIPCGHLVVCKDCAPSLRK-----CPICR 590
Cdd:cd16785    3 CTICYENVVDTVIYTCGHMCLCYTCGLKLKKmanacCPICR 43
RING-HC_RNF141 cd16545
RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins; ...
555-590 3.77e-03

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


Pssm-ID: 319459 [Multi-domain]  Cd Length: 39  Bit Score: 35.07  E-value: 3.77e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 163644309 555 CKVCMDREVSIVfIPCGHlVVCKDC----APSLRKCPICR 590
Cdd:cd16545    2 CCICMDRKPDTI-LPCAH-SFCQKCidkwSVRHRTCPICR 39
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
554-589 3.81e-03

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 316445 [Multi-domain]  Cd Length: 40  Bit Score: 35.09  E-value: 3.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 163644309  554 MCKVCMDR-EVSIVFIPCGHlVVCKDC-APSLR---KCPIC 589
Cdd:pfam13923   1 MCPICLDMlKDPSTTTPCGH-VFCQKCiLRALRsgnECPLC 40
RING-HC_BRE1_like cd16499
RING finger, HC subclass, found in yeast Bre1 and its homologs from eukaryotes; Bre1 is an E3 ...
554-590 6.16e-03

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


Pssm-ID: 319413 [Multi-domain]  Cd Length: 42  Bit Score: 34.49  E-value: 6.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 163644309 554 MCKVCMDREVSIVFIPCGHlVVCKDC-----APSLRKCPICR 590
Cdd:cd16499    2 KCSVCNDRQKDVILTKCGH-VFCKECiqerlETRQRKCPSCN 42
RING-HC_MEX3C cd16722
RING finger, HC subclass, found in RNA-binding protein MEX3C; MEX3C, also known as RING finger ...
555-590 7.64e-03

RING finger, HC subclass, found in RNA-binding protein MEX3C; MEX3C, also known as RING finger and KH domain-containing protein 2 (RKHD2), or RING finger protein 194 (RNF194), is a RNA-binding phosphoprotein that acts as a suppressor of chromosomal instability. It functions as a RNA-binding ubiquitin E3 ligase responsible for the post-transcriptional, HLA-A allotype-specific regulation of MHC class I molecules (MHC-I). It also modifies retinoic acid inducible gene-1 (RIG-I) in stress granules and plays a critical role in eliciting antiviral immune responses. Moreover, MEX3C plays an essential role in normal postnatal growth via enhancing the local expression of insulin-like growth factor 1 (IGF1) in bone. It may also be involved in metabolic regulation of energy balance. MEX3C 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, MEX3C shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway.


Pssm-ID: 319636  Cd Length: 43  Bit Score: 34.58  E-value: 7.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 163644309 555 CKVCMDREVSIVFIPCGHLVVCKDCA-----PSLRKCPICR 590
Cdd:cd16722    3 CVICFENEVIAALVPCGHNLFCMECAnkiceKDTPSCPVCQ 43
mRING-HC-C3HC5_RNF157 cd16817
Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 157 (RNF157) and ...
555-590 8.98e-03

Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 157 (RNF157) and similar proteins; RNF157 is a cytoplasmic E3 ubiquitin ligase predominantly expressed in brain. It is a homolog of the E3 ligase mahogunin ring finger-1 (MGRN1). In cultured neurons, it promotes neuronal survival in an E3 ligase-dependent manner. In contrast, it supports growth and maintenance of dendrites independent of its E3 ligase activity. RNF157 interacts with and ubiquitinates the adaptor protein APBB1 (amyloid beta precursor protein-binding, family B, member 1 or Fe65), which regulates neuronal survival, but not dendritic growth downstream of RNF157. The nuclear localization of APBB1 together with its interaction partner RNA-binding protein SART3 (squamous cell carcinoma antigen recognized by T cells 3 or Tip110) is crucial to trigger apoptosis. RNF157 contains a modified C3HC5-type RING-HC finger, and a functionally uncharacterized region, known as domain associated with RING2 (DAR2), N-terminal to the RING finger. The C3HC5-type RING-HC finger is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 319731  Cd Length: 41  Bit Score: 34.27  E-value: 8.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 163644309 555 CKVCMDREVSIVFIPCGHLVVCKDCAPSLR----KCPICR 590
Cdd:cd16817    2 CVVCLSDVRDTLILPCRHLCLCNACADTLRyqanNCPICR 41
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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