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Conserved domains on  [gi|2073512899|ref|XP_042560570|]
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uncharacterized protein LOC122129915 isoform X1 [Clupea harengus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPRY_PRY_SNTX cd16040
Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct ...
 1749-1929 3.48e-123

Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of Stonustoxin alpha proteins. Stonustoxin (SNTX) is a multifunctional lethal protein isolated from venom elaborated by the stonefish. It comprises two subunits, termed alpha and beta. SNTX elicits an array of biological responses, particularly a potent hypotension and respiratory difficulties.


:

Pssm-ID: 294002 [Multi-domain]  Cd Length: 180  Bit Score: 384.53  E-value: 3.48e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1749 KPGPRKYACELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGLSGRCYWEAEWSGDGAEIAVAY 1828
Cdd:cd16040      1 REEFLKYACQLTLDPNTAHRNLSLSEGNRKVTRVKEEQPYPDHPERFDYWPQVLCREGLSGRCYWEVEWSGGGVDIAVAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1829 KSIKRKEWSDESALGCNDKSWGLFCSPHGYYAKHNNEPTDIPVPSSRSSRVGVYLDWPAGTLSFYSVfSDTLTHLHTFHS 1908
Cdd:cd16040     81 KGISRKGDGDDSRFGYNDKSWSLECSPSGYSFWHNNKKTEISVPSSSSSRVGVYLDHSAGTLSFYSV-SDTMTLLHTVQT 159

                          170       180
                   ....*....|....*....|.
gi 2073512899 1909 TFTESLYPGFRVWPDSSVSLC 1929
Cdd:cd16040    160 TFTEPLYPGFGVGYGSSVKLC 180
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 883-1013 1.43e-35

NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein.


:

Pssm-ID: 465499 [Multi-domain]  Cd Length: 122  Bit Score: 132.03  E-value: 1.43e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  883 HLSIQEFLAALHVFASYLSKNMKALTPFLkgksrslpDVPLHELLKNAVNKALESKNGHLDLFVRFLHGISLESNQRLLV 962
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKEFF--------GLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLE 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2073512899  963 GLLThTHSSPESEKKTIRNLKVMQRPNISPERCINLFHCLVEMHDSSVHDE 1013
Cdd:pfam17776   73 GLLG-CKLSSEIKQELLQWIKSLIQKELSSERFLNLFHCLYELQDESFVKE 122
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 487-558 2.80e-31

Fish-specific NACHT associated domain; This domain is frequently found associated with the NACHT domain (pfam05729) in fish and other vertebrates.


:

Pssm-ID: 464185 [Multi-domain]  Cd Length: 72  Bit Score: 117.71  E-value: 2.80e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2073512899  487 HKASMKRRFESISEGIIRSETQTLLNKIYTELYITEGESEGVNNEHEVWQVESASRSQTTEDTAINCNDIFK 558
Cdd:pfam14484    1 LKSNLKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAASKKPESEETPIRCEDIFK 72
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 1340-1687 1.94e-30

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 319  Bit Score: 124.00  E-value: 1.94e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1340 LKILRLKGCKLTHESCKVVASFLQSANPLLELDLSNNVLR--DSGVQLLSKGLSSPhCKLQTLRLTDCHISDDGyvCLAL 1417
Cdd:cd00116     25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGriPRGLQSLLQGLTKG-CGLQELDLSDNALGPDG--CGVL 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1418 TLMANPSCVKELDLSNNNSGESAKNLLFATLKDPHLKMEELRLAGCKLTERSYEIVASALqSANSPLRELDLGHSDLQQS 1497
Cdd:cd00116    102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKAL-RANRDLKELNLANNGIGDA 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1498 G-EMLLSALQSpNCKLETLRLTGCKLT---GRFLALTLQgANPHLRELDISDgelqysggellhqplnqdCKVRLICCRl 1573
Cdd:cd00116    181 GiRALAEGLKA-NCNLEVLDLNNNGLTdegASALAETLA-SLKSLEVLNLGD------------------NNLTDAGAA- 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1574 kdsscavmasvlqfcvsqlsvldmtgcdlqtsdeKLLSCLGNPNCQLKTLKLADCKLTEESCKALASTLQSSVSLTELDL 1653
Cdd:cd00116    240 ----------------------------------ALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDL 285

                          330       340       350
                   ....*....|....*....|....*....|....
gi 2073512899 1654 TNSELKDSGIQLLSAGLSNPHCKLQTLRLSGCLI 1687
Cdd:cd00116    286 RGNKFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 568-736 1.60e-28

NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.


:

Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 113.55  E-value: 1.60e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  568 RTAMTKGIAGIGKTVSVQKFILDWAEEKANQDVDFMFILPFRVLNLVKhDQYSLHKLLLDFHPELRELQDGEYKDRC--- 644
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSG-NARSLADLLFSQWPEPAAPVSEVWAVILelp 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  645 --IVFIFDGLDESRlplnfqenQQLSDVTQTSSVDVLMTSLIQGSLLPSAHIWITSRPAAASQIPSQ-CINQVTEVRGFS 721
Cdd:pfam05729   80 erLLLILDGLDELV--------SDLGQLDGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGlEEPRYLEVRGFS 151

                          170
                   ....*....|....*
gi 2073512899  722 DPQKEEYFRKRISDQ 736
Cdd:pfam05729  152 ESDRKQYVRKYFSDE 166
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 1048-1460 8.96e-24

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 319  Bit Score: 104.36  E-value: 8.96e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1048 DEFDLKKYKTSPEGRRRLVPAVRCCRKALLADCKLSERSFEIVASALQsANSPLRELDLSHSDLQQSGEMLGSALQspnc 1127
Cdd:cd00116      1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALR-PQPSLKELCLSLNETGRIPRGLQSLLQ---- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1128 kletlrlagckltgrflALTlqgANPHLRELDISDGELQDCGgellhkplnedckvrlkhssCAVVASVLQfcVSQLSVL 1207
Cdd:cd00116     76 -----------------GLT---KGCGLQELDLSDNALGPDG--------------------CGVLESLLR--SSSLQEL 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1208 DMSGCDLQTSEEK-LPSSLGNPNCRLKTLRLAGCKLTGRF---LALTLQgANPHLRELDISDSELQDCGgellhqplnqe 1283
Cdd:cd00116    114 KLNNNGLGDRGLRlLAKGLKDLPPALEKLVLGRNRLEGASceaLAKALR-ANRDLKELNLANNGIGDAG----------- 181

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1284 ckVRLLCCRLKHsscavvasvlqfcvsqlsdldmsgcdpqtsvekllsslgnpNCRLKILRLKGCKLTHESCKVVASFLQ 1363
Cdd:cd00116    182 --IRALAEGLKA-----------------------------------------NCNLEVLDLNNNGLTDEGASALAETLA 218

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1364 SANPLLELDLSNNVLRDSGVQLLSKGLSSPHCKLQTLRLTDCHISDDGYVCLAlTLMANPSCVKELDLSNNNSGESAKNL 1443
Cdd:cd00116    219 SLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLA-EVLAEKESLLELDLRGNKFGEEGAQL 297

                          410
                   ....*....|....*..
gi 2073512899 1444 LFATLKDPHLKMEELRL 1460
Cdd:cd00116    298 LAESLLEPGNELESLWV 314
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 10-79 2.21e-17

Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. 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. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer.


The actual alignment was detected with superfamily member cd08321:

Pssm-ID: 472698  Cd Length: 82  Bit Score: 78.33  E-value: 2.21e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2073512899   10 REVLRNTLDNLTGAEFKRFKHYLQDQGQ-----IAWGKLEKADTDDTVDLMVQVYST-GAGDIILSILKTIKHNQL 79
Cdd:cd08321      1 RDLLLDALEDLGEEELKKFKWKLRDIPLegyprIPRGKLENADRVDLVDLLVSYYGEdYAVEVTVEVLRAINQNDL 76
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 821-881 2.19e-16

NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known.


:

Pssm-ID: 465501  Cd Length: 57  Bit Score: 74.91  E-value: 2.19e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2073512899  821 DVILKLAELAFKHLENGNLMFYEEDLKECGIDvsEASVYSGMCTEIFREEcvFHHKKVYCF 881
Cdd:pfam17779    1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLD--ESDLSSGLLTEILQKD--LGCEKVYSF 57
RING_Ubox super family cl17238
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
 317-362 1.36e-14

RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enable efficient transfer of ubiquitin from E2 to the substrates.


The actual alignment was detected with superfamily member cd16601:

Pssm-ID: 473075 [Multi-domain]  Cd Length: 44  Bit Score: 69.44  E-value: 1.36e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2073512899  317 QSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSgpSGDYSCPQC 362
Cdd:cd16601      1 EASCSLCKEYLKDPVIIECGHNFCRACITRFWEEL--DGDFPCPQC 44
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 183-469 5.54e-09

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 61.32  E-value: 5.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  183 QIGRGPSSSDKPQTHRPVSPVPSCVSMKSDWSMGRPPNFSSGPPQ-----SDPKPQTHRPVSP---VPSCVSMKSDR--- 251
Cdd:pfam03154  165 QILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQgspatSQPPNQTQSTAAPhtlIQQTPTLHPQRlps 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  252 ------SMGRPPNFSNGPPQSDPKPQTHRPVSPVPScvSMKSDRSMGRPPnfsnGPPQSDPnvwrnvLTQDQSRCgvceQ 325
Cdd:pfam03154  245 phpplqPMTQPPPPSQVSPQPLPQPSLHGQMPPMPH--SLQTGPSHMQHP----VPPQPFP------LTPQSSQS----Q 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  326 LLRDPVITTCGHSFCRQcissywsQSGPSgdYSCPQCRKRSRAQPsLNPditmaQPLlyahtttTQPHVYPPTAMAQSSL 405
Cdd:pfam03154  309 VPPGPSPAAPGQSQQRI-------HTPPS--QSQLQSQQPPREQP-LPP-----APL-------SMPHIKPPPTTPIPQL 366

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2073512899  406 yqhremaqhhlkPSTTMAQVPPHSdSGQDPlyphFHMAQISPQPPldehiVLEGSKHLQTEHAP 469
Cdd:pfam03154  367 ------------PNPQSHKHPPHL-SGPSP----FQMNSNLPPPP-----ALKPLSSLSTHHPP 408
FISNA super family cl20537
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 139-194 6.12e-03

Fish-specific NACHT associated domain; This domain is frequently found associated with the NACHT domain (pfam05729) in fish and other vertebrates.


The actual alignment was detected with superfamily member pfam14484:

Pssm-ID: 464185 [Multi-domain]  Cd Length: 72  Bit Score: 37.21  E-value: 6.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2073512899  139 LQEHLKQRFSVVH----QESGVSSVQDIYTDLHIVEGRTGEVST-NNMSQIG---RGPSSSDKP 194
Cdd:pfam14484    1 LKSNLKKKFQCIFegnaKGGESTLLNEIYTELYITEGESGEVNEeHEVRQIEaasKKPESEETP 64
 
Name Accession Description Interval E-value
SPRY_PRY_SNTX cd16040
Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct ...
 1749-1929 3.48e-123

Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of Stonustoxin alpha proteins. Stonustoxin (SNTX) is a multifunctional lethal protein isolated from venom elaborated by the stonefish. It comprises two subunits, termed alpha and beta. SNTX elicits an array of biological responses, particularly a potent hypotension and respiratory difficulties.


Pssm-ID: 294002 [Multi-domain]  Cd Length: 180  Bit Score: 384.53  E-value: 3.48e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1749 KPGPRKYACELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGLSGRCYWEAEWSGDGAEIAVAY 1828
Cdd:cd16040      1 REEFLKYACQLTLDPNTAHRNLSLSEGNRKVTRVKEEQPYPDHPERFDYWPQVLCREGLSGRCYWEVEWSGGGVDIAVAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1829 KSIKRKEWSDESALGCNDKSWGLFCSPHGYYAKHNNEPTDIPVPSSRSSRVGVYLDWPAGTLSFYSVfSDTLTHLHTFHS 1908
Cdd:cd16040     81 KGISRKGDGDDSRFGYNDKSWSLECSPSGYSFWHNNKKTEISVPSSSSSRVGVYLDHSAGTLSFYSV-SDTMTLLHTVQT 159

                          170       180
                   ....*....|....*....|.
gi 2073512899 1909 TFTESLYPGFRVWPDSSVSLC 1929
Cdd:cd16040    160 TFTEPLYPGFGVGYGSSVKLC 180
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 883-1013 1.43e-35

NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein.


Pssm-ID: 465499 [Multi-domain]  Cd Length: 122  Bit Score: 132.03  E-value: 1.43e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  883 HLSIQEFLAALHVFASYLSKNMKALTPFLkgksrslpDVPLHELLKNAVNKALESKNGHLDLFVRFLHGISLESNQRLLV 962
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKEFF--------GLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLE 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2073512899  963 GLLThTHSSPESEKKTIRNLKVMQRPNISPERCINLFHCLVEMHDSSVHDE 1013
Cdd:pfam17776   73 GLLG-CKLSSEIKQELLQWIKSLIQKELSSERFLNLFHCLYELQDESFVKE 122
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 487-558 2.80e-31

Fish-specific NACHT associated domain; This domain is frequently found associated with the NACHT domain (pfam05729) in fish and other vertebrates.


Pssm-ID: 464185 [Multi-domain]  Cd Length: 72  Bit Score: 117.71  E-value: 2.80e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2073512899  487 HKASMKRRFESISEGIIRSETQTLLNKIYTELYITEGESEGVNNEHEVWQVESASRSQTTEDTAINCNDIFK 558
Cdd:pfam14484    1 LKSNLKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAASKKPESEETPIRCEDIFK 72
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 1340-1687 1.94e-30

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 124.00  E-value: 1.94e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1340 LKILRLKGCKLTHESCKVVASFLQSANPLLELDLSNNVLR--DSGVQLLSKGLSSPhCKLQTLRLTDCHISDDGyvCLAL 1417
Cdd:cd00116     25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGriPRGLQSLLQGLTKG-CGLQELDLSDNALGPDG--CGVL 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1418 TLMANPSCVKELDLSNNNSGESAKNLLFATLKDPHLKMEELRLAGCKLTERSYEIVASALqSANSPLRELDLGHSDLQQS 1497
Cdd:cd00116    102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKAL-RANRDLKELNLANNGIGDA 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1498 G-EMLLSALQSpNCKLETLRLTGCKLT---GRFLALTLQgANPHLRELDISDgelqysggellhqplnqdCKVRLICCRl 1573
Cdd:cd00116    181 GiRALAEGLKA-NCNLEVLDLNNNGLTdegASALAETLA-SLKSLEVLNLGD------------------NNLTDAGAA- 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1574 kdsscavmasvlqfcvsqlsvldmtgcdlqtsdeKLLSCLGNPNCQLKTLKLADCKLTEESCKALASTLQSSVSLTELDL 1653
Cdd:cd00116    240 ----------------------------------ALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDL 285

                          330       340       350
                   ....*....|....*....|....*....|....
gi 2073512899 1654 TNSELKDSGIQLLSAGLSNPHCKLQTLRLSGCLI 1687
Cdd:cd00116    286 RGNKFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 568-736 1.60e-28

NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 113.55  E-value: 1.60e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  568 RTAMTKGIAGIGKTVSVQKFILDWAEEKANQDVDFMFILPFRVLNLVKhDQYSLHKLLLDFHPELRELQDGEYKDRC--- 644
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSG-NARSLADLLFSQWPEPAAPVSEVWAVILelp 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  645 --IVFIFDGLDESRlplnfqenQQLSDVTQTSSVDVLMTSLIQGSLLPSAHIWITSRPAAASQIPSQ-CINQVTEVRGFS 721
Cdd:pfam05729   80 erLLLILDGLDELV--------SDLGQLDGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGlEEPRYLEVRGFS 151

                          170
                   ....*....|....*
gi 2073512899  722 DPQKEEYFRKRISDQ 736
Cdd:pfam05729  152 ESDRKQYVRKYFSDE 166
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 1048-1460 8.96e-24

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 104.36  E-value: 8.96e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1048 DEFDLKKYKTSPEGRRRLVPAVRCCRKALLADCKLSERSFEIVASALQsANSPLRELDLSHSDLQQSGEMLGSALQspnc 1127
Cdd:cd00116      1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALR-PQPSLKELCLSLNETGRIPRGLQSLLQ---- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1128 kletlrlagckltgrflALTlqgANPHLRELDISDGELQDCGgellhkplnedckvrlkhssCAVVASVLQfcVSQLSVL 1207
Cdd:cd00116     76 -----------------GLT---KGCGLQELDLSDNALGPDG--------------------CGVLESLLR--SSSLQEL 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1208 DMSGCDLQTSEEK-LPSSLGNPNCRLKTLRLAGCKLTGRF---LALTLQgANPHLRELDISDSELQDCGgellhqplnqe 1283
Cdd:cd00116    114 KLNNNGLGDRGLRlLAKGLKDLPPALEKLVLGRNRLEGASceaLAKALR-ANRDLKELNLANNGIGDAG----------- 181

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1284 ckVRLLCCRLKHsscavvasvlqfcvsqlsdldmsgcdpqtsvekllsslgnpNCRLKILRLKGCKLTHESCKVVASFLQ 1363
Cdd:cd00116    182 --IRALAEGLKA-----------------------------------------NCNLEVLDLNNNGLTDEGASALAETLA 218

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1364 SANPLLELDLSNNVLRDSGVQLLSKGLSSPHCKLQTLRLTDCHISDDGYVCLAlTLMANPSCVKELDLSNNNSGESAKNL 1443
Cdd:cd00116    219 SLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLA-EVLAEKESLLELDLRGNKFGEEGAQL 297

                          410
                   ....*....|....*..
gi 2073512899 1444 LFATLKDPHLKMEELRL 1460
Cdd:cd00116    298 LAESLLEPGNELESLWV 314
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
456-912 3.86e-22

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 104.50  E-value: 3.86e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  456 VLEGSKHLQTEHAPVKRAKLRDDILNRALVNHKASMKRRFESISegIIRSETQTLLNKIYTELYITEGESEGVNNEHEVW 535
Cdd:COG5635     66 ALSAAALLARALSALLLVLLLLESLLLLLLLLLLLAEALLALLE--LAALLKAVLLSLSGGSDLVLLLSESDLLLALLIL 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  536 QVESASRSQTTEDTAINCNDIFKSLPGQQRPIRTAMTK-----GIAGIGKTVSVQKFILDWAEEKANQDVDFMFILPFR- 609
Cdd:COG5635    144 LLDADGLLVSLDDLYVPLNLLERIESLKRLELLEAKKKrllilGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRd 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  610 ------VLNLVKHdqySLHKLLLDFHPELRELQDgeyKDRCiVFIFDGLDESRLPLNFQEN-QQLSDVTQTssvdvlmts 682
Cdd:COG5635    224 laeeasLEDLLAE---ALEKRGGEPEDALERLLR---NGRL-LLLLDGLDEVPDEADRDEVlNQLRRFLER--------- 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  683 liqgslLPSAHIWITSRPAAAsqiPSQCINQVTEVR--GFSDPQKEEYFRKRI-SDQNQANRIISHIKASRSLYIMCHMP 759
Cdd:COG5635    288 ------YPKARVIITSRPEGY---DSSELEGFEVLElaPLSDEQIEEFLKKWFeATERKAERLLEALEENPELRELARNP 358

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  760 VFCWISATVLQqileedDGKEPPKTLTEMFIHFL--LIQTTRKKQKYQEENDIERQRLLEshkdvilKLAELAFKHLENG 837
Cdd:COG5635    359 LLLTLLALLLR------ERGELPDTRAELYEQFVelLLERWDEQRGLTIYRELSREELRE-------LLSELALAMQENG 425

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2073512899  838 NLMFYEEDLKECGIDVSEASVYSG-MCTEIFREECVFHHK--KVYCFVHLSIQEFLAALHVFASYLSKNMKALTPFLK 912
Cdd:COG5635    426 RTEFAREELEEILREYLGRRKDAEaLLDELLLRTGLLVERgeGRYSFAHRSFQEYLAARALVEELDEELLELLAEHLE 503
PRY pfam13765
SPRY-associated domain; PRY is a 50-60 amino acids domain associated with SPRY domains, ...
 1759-1807 2.87e-21

SPRY-associated domain; PRY is a 50-60 amino acids domain associated with SPRY domains, adjacent to its N-terminal. PRY and SPRY domains are structurally very similar and consist of a beta sandwich fold. Distant homologs are domains in butyrophilin/marenostrin/pyrin, evolutionarily more ancient than SPRY/B30.2 counterpart.


Pssm-ID: 463976  Cd Length: 49  Bit Score: 88.30  E-value: 2.87e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2073512899 1759 LTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL 1807
Cdd:pfam13765    1 VTLDPNTAHPSLVLSEDLKSVRYGDERQNVPDNPERFDSWPCVLGSEGF 49
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1808-1931 7.74e-21

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 89.66  E-value: 7.74e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  1808 SGRCYWEAEWSGDGA-EIAVAYKSIKRKewsDESALGCNDKSWGLF-CSPHGYyakHNNEPTDIPVPSSRS-SRVGVYLD 1884
Cdd:smart00449    1 SGRHYFEVEIGDGGHwRVGVATKSVPRG---YFALLGEDKGSWGYDgDGGKKY---HNSTGPEYGLPLQEPgDVIGCFLD 74

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 2073512899  1885 WPAGTLSFYSVfSDTLTHLHTFHSTFTESLYPGFRVWPDSS--VSLCQI 1931
Cdd:smart00449   75 LEAGTISFYKN-GKYLHGLAFFDVKFSGPLYPAFSLGSGNSvrLNFGPL 122
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 10-79 2.21e-17

Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated speck-like protein containing a CARD) and similar proteins. ASC is an adaptor molecule that functions in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. ASC contains two domains from the Death Domain (DD) superfamily, an N-terminal pyrin-like domain and a C-terminal Caspase activation and recruitment domain (CARD). Through these 2 domains, ASC serves as an adaptor for inflammasome integrity and oligomerizes to form supramolecular assemblies. Included in this family is human PYNOD (also known as NLRP10 or NOD8) which via its Pyrin domain suppresses oligomerization of ASC, and ASC-mediated NF-kappaB activation. Other members of this subfamily are associated with ATPase domains and their function remains unknown. In general, Pyrin is a subfamily of the DD superfamily and functions in several signaling pathways. 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 CARD and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260033  Cd Length: 82  Bit Score: 78.33  E-value: 2.21e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2073512899   10 REVLRNTLDNLTGAEFKRFKHYLQDQGQ-----IAWGKLEKADTDDTVDLMVQVYST-GAGDIILSILKTIKHNQL 79
Cdd:cd08321      1 RDLLLDALEDLGEEELKKFKWKLRDIPLegyprIPRGKLENADRVDLVDLLVSYYGEdYAVEVTVEVLRAINQNDL 76
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 1398-1729 5.53e-17

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 86.00  E-value: 5.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1398 QTLRLTDCHISDDGYVCLALTLMANPscVKELDLSNNNSG-ESAKNLLFATLKDPHLKMeeLRLAGCKLTERSYEIVASA 1476
Cdd:COG5238    156 VHLLGLAARLGLLAAISMAKALQNNS--VETVYLGCNQIGdEGIEELAEALTQNTTVTT--LWLKRNPIGDEGAEILAEA 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1477 LQSaNSPLRELDLGHSDLQQSGEMLLS-ALQSpNCKLETLRLTGCKLT---GRFLALTLQGaNPHLRELDISDGELQYSG 1552
Cdd:COG5238    232 LKG-NKSLTTLDLSNNQIGDEGVIALAeALKN-NTTVETLYLSGNQIGaegAIALAKALQG-NTTLTSLDLSVNRIGDEG 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1553 GELLHQPLNQdckvrliccrlkdsscavmasvlqfcvsqlsvldmtgcdlqtsdekllsclgnpNCQLKTLKLADCKLTE 1632
Cdd:COG5238    309 AIALAEGLQG------------------------------------------------------NKTLHTLNLAYNGIGA 334

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1633 ESCKALASTLQSSVSLTELDLTNSELKDSGIQLLSAGLSNpHCKLQTLRLSGCLITHQGCSFLASALKSNPfyLKQLDLS 1712
Cdd:COG5238    335 QGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEG-NTTLRELNLGKNNIGKQGAEALIDALQTNR--LHTLILD 411

                          330
                   ....*....|....*..
gi 2073512899 1713 YNHPGDSGVRELTDRLN 1729
Cdd:COG5238    412 GNLIGAEAQQRLEQLLE 428
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 821-881 2.19e-16

NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known.


Pssm-ID: 465501  Cd Length: 57  Bit Score: 74.91  E-value: 2.19e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2073512899  821 DVILKLAELAFKHLENGNLMFYEEDLKECGIDvsEASVYSGMCTEIFREEcvFHHKKVYCF 881
Cdd:pfam17779    1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLD--ESDLSSGLLTEILQKD--LGCEKVYSF 57
RING-HC_TRIM39_C-IV cd16601
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ...
 317-362 1.36e-14

RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar proteins; TRIM39, also known as RING finger protein 23 (RNF23) or testis-abundant finger protein, is an E3 ubiquitin-protein ligase that plays a role in controlling DNA damage-induced apoptosis through inhibition of the anaphase promoting complex (APC/C), a multiprotein ubiquitin ligase that controls multiple cell cycle regulators, including cyclins, geminin, and others. TRIM39 also functions as a regulator of several key processes in the proliferative cycle. It directly regulates p53 stability. It modulates cell cycle progression and DNA damage responses via stabilizing p21. Moreover, TRIM39 negatively regulates the nuclear factor kappaB (NFkappaB)-mediated signaling pathway through stabilization of Cactin, an inhibitor of NFkappaB- and Toll-like receptor (TLR)-mediated transcription, which is induced by inflammatory stimulants such as tumor necrosis factor alpha. Furthermore, TRIM39 is a MOAP-1-binding protein that can promote apoptosis signaling through stabilization of MOAP-1 via the inhibition of its poly-ubiquitination process. TRIM39 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438263 [Multi-domain]  Cd Length: 44  Bit Score: 69.44  E-value: 1.36e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2073512899  317 QSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSgpSGDYSCPQC 362
Cdd:cd16601      1 EASCSLCKEYLKDPVIIECGHNFCRACITRFWEEL--DGDFPCPQC 44
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 13-79 2.71e-14

PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the same fold as the pfam00531 domain. This similarity may mean that this is a protein-protein interaction domain.


Pssm-ID: 460678  Cd Length: 76  Bit Score: 69.54  E-value: 2.71e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2073512899   13 LRNTLDNLTGAEFKRFKHYLQD-----QGQIAWGKLEKADTDDTVDLMVQVYSTGAG-DIILSILKTIKHNQL 79
Cdd:pfam02758    2 LLWYLEELSEEEFKKFKSLLEDepeegLRSIPRGKLEKADRLDLADLLVEHYGEDAAvDVTIEILKKINLKDL 74
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 183-469 5.54e-09

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 61.32  E-value: 5.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  183 QIGRGPSSSDKPQTHRPVSPVPSCVSMKSDWSMGRPPNFSSGPPQ-----SDPKPQTHRPVSP---VPSCVSMKSDR--- 251
Cdd:pfam03154  165 QILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQgspatSQPPNQTQSTAAPhtlIQQTPTLHPQRlps 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  252 ------SMGRPPNFSNGPPQSDPKPQTHRPVSPVPScvSMKSDRSMGRPPnfsnGPPQSDPnvwrnvLTQDQSRCgvceQ 325
Cdd:pfam03154  245 phpplqPMTQPPPPSQVSPQPLPQPSLHGQMPPMPH--SLQTGPSHMQHP----VPPQPFP------LTPQSSQS----Q 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  326 LLRDPVITTCGHSFCRQcissywsQSGPSgdYSCPQCRKRSRAQPsLNPditmaQPLlyahtttTQPHVYPPTAMAQSSL 405
Cdd:pfam03154  309 VPPGPSPAAPGQSQQRI-------HTPPS--QSQLQSQQPPREQP-LPP-----APL-------SMPHIKPPPTTPIPQL 366

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2073512899  406 yqhremaqhhlkPSTTMAQVPPHSdSGQDPlyphFHMAQISPQPPldehiVLEGSKHLQTEHAP 469
Cdd:pfam03154  367 ------------PNPQSHKHPPHL-SGPSP----FQMNSNLPPPP-----ALKPLSSLSTHHPP 408
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 1091-1410 6.19e-09

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 60.57  E-value: 6.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1091 ASALQSANSPLRELDLSHSDLQQSgemLGSALQSPNcklETLRLAGCKLTGRFLALTLQ-GANPHLRELDISDGELQDCG 1169
Cdd:COG5238    123 MAKTLEDSLILYLALPRRINLIQV---LKDPLGGNA---VHLLGLAARLGLLAAISMAKaLQNNSVETVYLGCNQIGDEG 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1170 GELLHKPLNEDCKVR---LKHSSCA-----VVASVLQFcVSQLSVLDMSGCDLQTSE-EKLPSSLGNpNCRLKTLRLAGC 1240
Cdd:COG5238    197 IEELAEALTQNTTVTtlwLKRNPIGdegaeILAEALKG-NKSLTTLDLSNNQIGDEGvIALAEALKN-NTTVETLYLSGN 274

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1241 KLT---GRFLALTLQGaNPHLRELDISDSELQDCGGELLHQPLNQECKVRLLCcrLKHSscavvasvlqfcvsQLSDldm 1317
Cdd:COG5238    275 QIGaegAIALAKALQG-NTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLN--LAYN--------------GIGA--- 334

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1318 SGCdpqtsvEKLLSSLgNPNCRLKILRLKGCKLTHESCKVVASFLQSANPLLELDLSNNVLRDSGVQLLSKGLSspHCKL 1397
Cdd:COG5238    335 QGA------IALAKAL-QENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQ--TNRL 405

                          330
                   ....*....|...
gi 2073512899 1398 QTLRLTDCHISDD 1410
Cdd:COG5238    406 HTLILDGNLIGAE 418
zf-C3HC4_4 pfam15227
zinc finger of C3HC4-type, RING; This is a family of primate-specific Ret finger protein-like ...
 320-362 7.70e-09

zinc finger of C3HC4-type, RING; This is a family of primate-specific Ret finger protein-like (RFPL) zinc-fingers of the C3HC4 type. Ret finger protein-like proteins are primate-specific target genes of Pax6, a key transcription factor for pancreas, eye and neocortex development. This domain is likely to be DNA-binding. This zinc-finger domain together with the RDM domain, pfam11002, forms a large zinc-finger structure of the RING/U-Box superfamily. RING-containing proteins are known to exert an E3 ubiquitin protein ligase activity with the zinc-finger structure being mandatory for binding to the E2 ubiquitin-conjugating enzyme.


Pssm-ID: 464570 [Multi-domain]  Cd Length: 42  Bit Score: 52.82  E-value: 7.70e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWsQSGPSGDYSCPQC 362
Cdd:pfam15227    1 CPICLDYLEKPVSIECGHSFCLSCINSLQ-KEPDGESLLCPQC 42
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 320-362 2.55e-08

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: 51.36  E-value: 2.55e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 2073512899   320 CGVC-EQLLRDPVITTCGHSFCRQCISSYWSQSGPsgdySCPQC 362
Cdd:smart00184    1 CPIClEEYLKDPVILPCGHTFCRSCIRKWLESGNN----TCPIC 40
COG5222 COG5222
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
303-378 6.64e-08

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227547 [Multi-domain]  Cd Length: 427  Bit Score: 57.06  E-value: 6.64e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2073512899  303 QSDPN-VWRNVLTQDQSRCGVCEQLLRDPVIT-TCGHSFCRQCISSYWSQSgpsgDYSCPQCRKRSRAQPSLNPDITM 378
Cdd:COG5222    259 AEIPDqVYKMQPPNISLKCPLCHCLLRNPMKTpCCGHTFCDECIGTALLDS----DFKCPNCSRKDVLLDGLTPDIDK 332
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
 316-363 9.86e-07

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 53.47  E-value: 9.86e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2073512899  316 DQS-RCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGpsgdySCPQCR 363
Cdd:TIGR00599   24 DTSlRCHICKDFFDVPVLTSCSHTFCSLCIRRCLSNQP-----KCPLCR 67
PHA03247 PHA03247
large tegument protein UL36; Provisional
 182-451 1.41e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  182 SQIGRGPSSSDKPQTHRPVSPVPSCVSMKSdwsMGRPPnfssgPPQSDPKPQTHRPVSPVPSCVSMKSDRSMGRPPNFSN 261
Cdd:PHA03247  2668 RRLGRAAQASSPPQRPRRRAARPTVGSLTS---LADPP-----PPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAP 2739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  262 GPPqsdPKPQThrPVSPVpscvsmkSDRSMGRPPNFSnGPPQSDPnvwrnvltqdqSRCGVCEQLLRDPVITTCGHSFCR 341
Cdd:PHA03247  2740 APP---AVPAG--PATPG-------GPARPARPPTTA-GPPAPAP-----------PAAPAAGPPRRLTRPAVASLSESR 2795

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  342 QCISSYWSQSGPSGDYSCPQCRKRSRAQPS-LNPDITMAQPLL-------YAHTTTTQPHVYP-------------PTAM 400
Cdd:PHA03247  2796 ESLPSPWDPADPPAAVLAPAAALPPAASPAgPLPPPTSAQPTApppppgpPPPSLPLGGSVAPggdvrrrppsrspAAKP 2875

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2073512899  401 AQSSLYQHREMAQHHLKPSTTMAQVPPHS-------DSGQDPLYPHFHMAQISPQPPL 451
Cdd:PHA03247  2876 AAPARPPVRRLARPAVSRSTESFALPPDQperppqpQAPPPPQPQPQPPPPPQPQPPP 2933
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
1617-1644 2.87e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 37.00  E-value: 2.87e-03
                            10        20
                    ....*....|....*....|....*...
gi 2073512899  1617 NCQLKTLKLADCKLTEESCKALASTLQS 1644
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
PLN03208 PLN03208
E3 ubiquitin-protein ligase RMA2; Provisional
 320-354 5.57e-03

E3 ubiquitin-protein ligase RMA2; Provisional


Pssm-ID: 178747 [Multi-domain]  Cd Length: 193  Bit Score: 40.07  E-value: 5.57e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPS 354
Cdd:PLN03208    21 CNICLDQVRDPVVTLCGHLFCWPCIHKWTYASNNS 55
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 139-194 6.12e-03

Fish-specific NACHT associated domain; This domain is frequently found associated with the NACHT domain (pfam05729) in fish and other vertebrates.


Pssm-ID: 464185 [Multi-domain]  Cd Length: 72  Bit Score: 37.21  E-value: 6.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2073512899  139 LQEHLKQRFSVVH----QESGVSSVQDIYTDLHIVEGRTGEVST-NNMSQIG---RGPSSSDKP 194
Cdd:pfam14484    1 LKSNLKKKFQCIFegnaKGGESTLLNEIYTELYITEGESGEVNEeHEVRQIEaasKKPESEETP 64
 
Name Accession Description Interval E-value
SPRY_PRY_SNTX cd16040
Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct ...
 1749-1929 3.48e-123

Stonustoxin subunit alpha or SNTX subunit alpha; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of Stonustoxin alpha proteins. Stonustoxin (SNTX) is a multifunctional lethal protein isolated from venom elaborated by the stonefish. It comprises two subunits, termed alpha and beta. SNTX elicits an array of biological responses, particularly a potent hypotension and respiratory difficulties.


Pssm-ID: 294002 [Multi-domain]  Cd Length: 180  Bit Score: 384.53  E-value: 3.48e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1749 KPGPRKYACELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGLSGRCYWEAEWSGDGAEIAVAY 1828
Cdd:cd16040      1 REEFLKYACQLTLDPNTAHRNLSLSEGNRKVTRVKEEQPYPDHPERFDYWPQVLCREGLSGRCYWEVEWSGGGVDIAVAY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1829 KSIKRKEWSDESALGCNDKSWGLFCSPHGYYAKHNNEPTDIPVPSSRSSRVGVYLDWPAGTLSFYSVfSDTLTHLHTFHS 1908
Cdd:cd16040     81 KGISRKGDGDDSRFGYNDKSWSLECSPSGYSFWHNNKKTEISVPSSSSSRVGVYLDHSAGTLSFYSV-SDTMTLLHTVQT 159

                          170       180
                   ....*....|....*....|.
gi 2073512899 1909 TFTESLYPGFRVWPDSSVSLC 1929
Cdd:cd16040    160 TFTEPLYPGFGVGYGSSVKLC 180
SPRY_PRY_C-I_2 cd12891
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, ...
 1759-1929 3.85e-68

PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM14-like, TRIM16-like, TRIM25-like, TRIM47-like, TRIM65 and RNF135, and stonustoxin; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class I TRIM proteins, including TRIM14, TRIM16 and TRIM25, TRIM47 as well as RING finger protein RNF135 and stonustoxin, a secreted poisonous protein of the stonefish Synanceja horrida. TRIM16 (also known as estrogen-responsive B box protein or EBBP) has E3 ubiquitin ligase activity. It is a regulator of keratinocyte differentiation and a tumor suppressor in retinoid-sensitive neuroblastoma. TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function. TRIM47, also known as GOA (Gene overexpressed in astrocytoma protein) or RNF100 (RING finger protein 100), is highly expressed in kidney tubular cells, but low expressed in most tissue. It is overexpressed in astrocytoma tumor cells and plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. RNF135 ubiquitinates RIG-I (retinoic acid-inducible gene-I) to promote interferon-beta induction during the early phase of viral infection. Stonustoxin (STNX) is a hypotensive and lethal protein factor that also possesses other biological activities such as species-specific hemolysis (due to its ability to form pores in the cell membrane) and platelet aggregation, edema-induction, and endothelium-dependent vasorelaxation (mediated by the nitric oxide pathway and activation of potassium channels). The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293949 [Multi-domain]  Cd Length: 167  Bit Score: 226.74  E-value: 3.85e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1759 LTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWsQVLCREGL-SGRCYWEAEWSGDG-AEIAVAYKSIKRKEw 1836
Cdd:cd12891      1 LTLDPNTAHNNLALSGDLKTVTCSSENQHYPDSPERFTHS-QVLSTQSFsSGRHYWEVEVSESGgWSVGVAYPSIERKG- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1837 sDESALGCNDKSWGLFCSPHGYYAKHNNEPTDIPVPSSRssRVGVYLDWPAGTLSFYSVfSDTLTHLHTFHSTFTESLYP 1916
Cdd:cd12891     79 -DESRIGRNDKSWCLEWQDKSFSAWHNNEETPLPSVSSR--RLGVYLDYEAGRLSFYEL-SDPIRHLHTFTATFTEPLHP 154

                          170
                   ....*....|...
gi 2073512899 1917 GFRVWPDSSVSLC 1929
Cdd:cd12891    155 AFWVLEGGWIRIK 167
SPRY_PRY cd12874
PRY/SPRY domain, also known as B30.2; This domain contains residues in the N-terminus that ...
 1759-1929 8.07e-52

PRY/SPRY domain, also known as B30.2; This domain contains residues in the N-terminus that form a distinct PRY domain structure such that the B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Among the TRIM proteins, also known as the N-terminal RING finger/B-box/coiled coil (RBCC) family, only Classes I and II contain the B30.2 domain that has evolved under positive selection. Class I TRIM proteins include multiple members involved in antiviral immunity at various levels of interferon signaling cascade. Among the 75 human TRIMs, roughly half enhance immune response, which they do at multiple levels in signaling pathways. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293934 [Multi-domain]  Cd Length: 168  Bit Score: 180.20  E-value: 8.07e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1759 LTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL-SGRCYWEAEWSGDGA-EIAVAYKSIKRKew 1836
Cdd:cd12874      1 LTFDPDTAHLNLILSDDLRSVRVGDISQHPPEPPPRFFECWQVLGSQSFsSGRHYWEVDVQDDSSwYVGVTYKSLPRK-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1837 SDESALGCNDKSWGLFCSPHGYYAKHNNEPTDIPVPSSRssRVGVYLDWPAGTLSFYSVfSDTLTHLHTFHSTFTESLYP 1916
Cdd:cd12874     79 GKMSNLGRNNGSWCLEWRENEFSAWHNNPETRLPVTPPR--RLGVFLDCDGGSLSFYGV-TDGVQLLYTFKAKFTEPLYP 155

                          170
                   ....*....|...
gi 2073512899 1917 GFRVWPDSSVSLC 1929
Cdd:cd12874    156 AFWLGEGSTLSIC 168
SPRY_PRY_TRIM16 cd12890
PRY/SPRY domain in tripartite motif-containing protein 16 (TRIM16); This domain, consisting of ...
 1754-1918 2.71e-49

PRY/SPRY domain in tripartite motif-containing protein 16 (TRIM16); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM16 and TRIM-like proteins. TRIM16 (also known as estrogen-responsive B box protein or EBBP) does not possess a RING domain like the other TRIM proteins, but contains two B-box domains and can heterodimerize with other TRIM proteins such as TRIM24, Promyelocytic leukemia (PML) protein and Midline-1 (MID1 or TRIM18). It is a regulator of keratinocyte differentiation and a tumor suppressor in retinoid-sensitive neuroblastoma. It has been shown that loss of TRIM16 expression plays an important role in the development of cutaneous squamous cell carcinoma (SCC) and is a determinant of retinoid sensitivity. TRIM16 also has E3 ubiquitin ligase activity.


Pssm-ID: 293948  Cd Length: 182  Bit Score: 173.42  E-value: 2.71e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1754 KYACELTLDPNTAYRTLSLSEGNRKVTCVTK-EQPYPDHPERFDFWSQVLCREGLS-GRCYWEAEWSGDGAEIAVAYKSI 1831
Cdd:cd12890      6 KYAYPLTFDPDTAHRYLRLTEDNRKVTNTTPwEHPYPDHPERFEHWRQVLSQQSLYlGRYYFEVEISGEGTYVGLTYKSI 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1832 KRKEWSDESALGCNDKSWGLFCSPHGYYAKHNNEPTdiPVPSSRSSRVGVYLDWPAGTLSFYSVFSDTLTHLHTFHSTFT 1911
Cdd:cd12890     86 DRKGSESNSCISGNNFSWCLQWNGKEFSAWHSDVET--PLKKGPFTRLGIYLDYPGGTLSFYGVEDDGMTLLHKFQCKFT 163


                   ....*..
gi 2073512899 1912 ESLYPGF 1918
Cdd:cd12890    164 EPLYPAF 170
SPRY_PRY_TRIM14 cd13738
PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14); This is a TRIM14 domain ...
 1759-1931 3.19e-41

PRY/SPRY domain of tripartite motif-binding protein 14 (TRIM14); This is a TRIM14 domain family contains residues in the N-terminus that form a distinct PRY domain structure such that the B30.2 domain consists of PRY and SPRY subdomains. TRIM14 domains have yet to be characterized. These B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. It belongs to Class IV TRIM protein family which has members involved in antiviral immunity at various levels of interferon signaling cascade.


Pssm-ID: 293973 [Multi-domain]  Cd Length: 173  Bit Score: 149.94  E-value: 3.19e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1759 LTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREG-LSGRCYWEA--EWSGDGAEIAVAYKSIKRKE 1835
Cdd:cd13738      1 PTLEPDTLHPRLRLSDDRLTVSCGWLGTLGLCPPQRFDKLWQVLSRDSfFSGRHYWEVdlQEAGAGWWVGAAYPSIGRKG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1836 WSDESALGCNDKSWGLFCSPHGYYAKHNNEPTDIpVPSSRSSRVGVYLDWPAGTLSFYSVfSDTLTHLHTFHSTFTESLY 1915
Cdd:cd13738     81 DSEAARLGWNRQSWCLKRYDLEYWAFHDGQRSRL-RPEDDPDRLGVFLDYEAGILSFYDV-TGGMTHLHTFRATFQEPLY 158

                          170
                   ....*....|....*.
gi 2073512899 1916 PGFRVWpDSSVSLCQI 1931
Cdd:cd13738    159 PALRLW-EGSISICKL 173
SPRY_PRY_C-I_1 cd13733
PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, ...
 1758-1925 8.28e-41

PRY/SPRY domain in tripartite motif-containing (TRIM) proteins, including TRIM5, TRIM6, TRIM7, TRIM10, TRIM11, TRIM17, TRIM20, TRIM21, TRIM27, TRIM35, TRIM38, TRIM41, TRIM50, TRIM58, TRIM60, TRIM62, TRIM69, TRIM72, NF7 and bloodthirsty; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class IV TRIM proteins, including TRIM7, TRIM35, TRIM41, TRIM50, TRIM62, TRIM69, TRIM72, TRIM protein NF7 and bloodthirsty (bty). TRIM7 interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. TRIM35 may play a role as a tumor suppressor and is implicated in the cell death mechanism. TRIM41 is localized to speckles in the cytoplasm and nucleus, and functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23. TRIM62 is involved in the morphogenesis of the mammary gland; loss of TRIM62 gene expression in breast is associated with increased risk of recurrence in early-onset breast cancer. TRIM69 is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. TRIM protein NF7, which also contains a chromodomain (CHD) at the N-terminus and an RFP (Ret finger protein)-like domain at the C-terminus, is required for its association with transcriptional units of RNA polymerase II which is mediated by a trimeric B box. In Xenopus oocyte, xNF7 has been identified as a nuclear microtubule-associated protein (MAP) whose microtubule-bundling activity, but not E3-ligase activity, contributes to microtubule organization and spindle integrity. Bloodthirsty (bty) is a novel gene identified in zebrafish and has been shown to likely play a role in in regulation of the terminal steps of erythropoiesis. TRIM72 has been shown to perform a critical function in membrane repair following acute muscle injury by nucleating the assembly of the repair machinery at injury sites. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293968 [Multi-domain]  Cd Length: 174  Bit Score: 148.78  E-value: 8.28e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1758 ELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL-SGRCYWEAEwSGDGAEIA--VAYKSIKRK 1834
Cdd:cd13733      1 DVTLDPDTAHPNLILSEDLKSVRYGDKRQNLPDNPERFDTCVCVLGSEGFsSGRHYWEVE-VGGKTDWDlgVARESVNRK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1835 EWSDES------ALGCNDKswglfcspHGYYAkHNNEPTDIPVpSSRSSRVGVYLDWPAGTLSFYSVfsDTLTHLHTFHS 1908
Cdd:cd13733     80 GKITLSpengywTVGLRNG--------NEYKA-LTSPSTPLSL-REKPQKVGVFLDYEEGQVSFYNV--DDGSHIYTFTD 147

                          170
                   ....*....|....*..
gi 2073512899 1909 TFTESLYPGFRVWPDSS 1925
Cdd:cd13733    148 CFTEKLYPYFSPCLNDG 164
SPRY_PRY_TRIM65 cd12896
PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of ...
 1754-1930 8.69e-41

PRY/SPRY domain in tripartite motif-containing domain 65 (TRIM65); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM65 proteins (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). The SPRY/PRY combination is a possible component of immune defense. This protein family has not been characterized.


Pssm-ID: 293953 [Multi-domain]  Cd Length: 182  Bit Score: 149.14  E-value: 8.69e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1754 KYACELTLDPNTAYRTLSLSEGNRKVT-CVTKEQPYPDHPERFDFWsQVLCREGLS-GRCYWEAEWSGDGAEIAVAYKSI 1831
Cdd:cd12896      7 KDYRNLTFDPRTANKYLELSRQNRRAKhGRSAARGVPASPGSFELW-QVQCTQSFQhGHHYWEVEVSSHSVTLGVTYPGL 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1832 KRKEWSDES-ALGCNDKSWGLFCSPHGYYAKHNNEPTDIPVPSSRssRVGVYLDWPAGTLSFYSVfSDTLTHLHTFHSTF 1910
Cdd:cd12896     86 PRHKQGGHKdNIGRNPCSWGLQIQEDSLQAWHNGRAQKLQGVSYR--LLGVDLDLEAGTLTFYGL-EPGTQRLHTFHAIF 162

                          170       180
                   ....*....|....*....|
gi 2073512899 1911 TESLYPGFRVWPDSSVSLCQ 1930
Cdd:cd12896    163 TQPLYPVFWLLEGRTLTLCH 182
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 883-1013 1.43e-35

NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein.


Pssm-ID: 465499 [Multi-domain]  Cd Length: 122  Bit Score: 132.03  E-value: 1.43e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  883 HLSIQEFLAALHVFASYLSKNMKALTPFLkgksrslpDVPLHELLKNAVNKALESKNGHLDLFVRFLHGISLESNQRLLV 962
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKEFF--------GLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLE 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2073512899  963 GLLThTHSSPESEKKTIRNLKVMQRPNISPERCINLFHCLVEMHDSSVHDE 1013
Cdd:pfam17776   73 GLLG-CKLSSEIKQELLQWIKSLIQKELSSERFLNLFHCLYELQDESFVKE 122
SPRY_PRY_TRIM7_like cd12888
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, ...
 1758-1929 6.33e-35

PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7)-like, including TRIM7, TRIM10, TRIM15, TRIM26, TRIM39, TRIM41; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several tripartite motif-containing (TRIM) proteins, including TRIM7 (also referred to as glycogenin-interacting protein, RING finger protein 90 or RNF90), TRIM10, TRIM15, TRIM26, TRIM39 and TRIM41. TRIM7 or GNIP interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. TRIM10 (also known as hematopoietic RING finger 1 (HERF1) or TRIM10/HERF1) plays a key role in definitive erythroid development; downregulation of the Spi-1/PU.1 oncogene induces the expression of TRIM10/HERF1, a key factor required for terminal erythroid cell differentiation and survival. Antiviral activity of TRIM15 is dependent on the ability of its B-box to interact with the MLV Gag precursor protein; downregulation of TRIM15, along with TRIM11, enhances virus release suggesting that these proteins contribute to the endogenous restriction of retroviruses in cells. Tripartite motif-containing 26 (TRIM26) function is as yet unknown; however, since it is localized in the human histocompatibility complex (MHC) class I region, TRIM26 may play a role in immune response although studies show no association between TRIM26 polymorphisms and the risk of aspirin-exacerbated respiratory disease. TRIM39 is a MOAP-1 (Modulator of Apoptosis)-binding protein that stabilizes MOAP-1 through inhibition of its poly-ubiquitination process. TRIM41 (also known as RING finger-interacting protein with C kinase or RINCK) functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.


Pssm-ID: 293946 [Multi-domain]  Cd Length: 169  Bit Score: 131.91  E-value: 6.33e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1758 ELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL-SGRCYWEAEwSGDGAEIA--VAYKSIKRK 1834
Cdd:cd12888      1 NVTLDPDTAHPRLVLSEDRKSVRWGDTRQDLPDNPERFDTWPCVLGCEGFtSGRHYWEVE-VGDGGGWAvgVARESVRRK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1835 EWSDESALGcndKSWGLFCSPHGYYAKHNNEPtdiPVP-SSRSSRVGVYLDWPAGTLSFYSVfsDTLTHLHTFHSTF--T 1911
Cdd:cd12888     80 GEISFSPEE---GIWAVGQWGGQYWALTSPET---PLPlSEVPRRIRVYLDYEGGQVAFFDA--DNEAPIFTFPPASfaG 151

                          170
                   ....*....|....*...
gi 2073512899 1912 ESLYPGFRVWPDSSVSLC 1929
Cdd:cd12888    152 ERIFPWFWVGKGSQLKLC 169
SPRY_PRY_TRIM39 cd13745
PRY/SPRY domain in tripartite motif-binding protein 39 (TRIM39) and TRIM39-like; This domain, ...
 1755-1918 5.85e-33

PRY/SPRY domain in tripartite motif-binding protein 39 (TRIM39) and TRIM39-like; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of pyrin, several tripartite motif-containing proteins (TRIMs), including E3 ubiquitin-protein ligase (TRIM21), RET finger protein (RFP)/tripartite motif protein 27 (TRIM27), as well as butyrophilin (Btns) and butyrophilin-like (Btnl) family members, with the exception of Btnl2. Btn and Btnl family members are novel regulators of immune responses, with many of the genes located within the MHC. They are implicated in T-cell inhibition and modulation of epithelial cell-T cell interactions. TRIM21 (also known as RO52, SSA1 or RNF81) is a major autoantigen in autoimmune diseases such as rheumatoid arthritis, systemic lupus erythematosus, and Sjorgen's syndrome. TRIM27 (also known as Ret finger protein, RFP or RNF76) negatively regulates CD4 T-cells by ubiquitinating and inhibiting the class II phosphatidylinositol 3 kinase C2beta (PI3K-C2beta), a kinase critical for KCa3.1 channel activation. The PRY/SPRY domain of Pyrin, which is mutated in familial Mediterranean fever patients, interacts with inflammasome components and inhibits proIL-1beta processing.


Pssm-ID: 293979 [Multi-domain]  Cd Length: 177  Bit Score: 126.59  E-value: 5.85e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1755 YACELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREG-LSGRCYWEAEwSGDGAE--IAVAYKSI 1831
Cdd:cd13745      1 FAVDVTLDPDTAHPNLVLSEDRKSVRHGDTRQDLPDNPERFDTYPCVLGAEGfTGGRHYWEVE-VGDKTEwtLGVCRESV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1832 KRKEWSDESAlgcNDKSWGLfCSPHGYYAKHNNEPTDIPVpSSRSSRVGVYLDWPAGTLSFYSVfSDTlTHLHTFHSTFT 1911
Cdd:cd13745     80 SRKGEVTLSP---ENGYWTV-WLRDGKYEALTSPPTPLPV-SVRPSRVGIFLDYEAGEVSFYNV-TDR-SHLFTFTDTFS 152


                   ....*..
gi 2073512899 1912 ESLYPGF 1918
Cdd:cd13745    153 GTLRPYF 159
SPRY_PRY_BTN1_2 cd15819
butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A); This domain, consisting of the ...
 1756-1928 1.82e-31

butyrophilin subfamily member A1 and A2 (BTN1A and BTN2A); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of butyrophilin family 1A and 2A (BTN1A and BTN2A). BTNs belong to receptor glycoproteins of immunoglobulin (Ig) superfamily, characterized by the presence of extracellular Ig-like domains (IgV and/or IgC). BTN1A plays a role in the secretion, formation and stabilization of milk fat globules. The B30.2 domain of BTN1A1 binds the enzyme xanthine oxidoreductase (XOR) in order to participate in milk fat globule secretion; this interaction may lead to the production of reactive oxygen species, which have immunomodulatory and antimicrobial functions. Duplication events have led to three paralogs of BTN2A in primates: BTN2A1, BTN2A2, and BTN2A3. In humans, only BTN2A1 has been functionally characterized; it has been detected on epithelial cells and leukocytes, and identified as a novel ligand of dendritic cell-specific ICAM-3 grabbing nonintegrin (DCSIGN), a C-type lectin receptor that acts as an internalization receptor for HIV-1, HCV, and other pathogens. BTN2A2 mRNA has been shown to be expressed in circulating human immune cells.


Pssm-ID: 293991 [Multi-domain]  Cd Length: 172  Bit Score: 121.95  E-value: 1.82e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1756 ACELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL-SGRCYWEAEwSGDgaeiavayksikRK 1834
Cdd:cd15819      1 AVNVTLDPDTAHPALILSEDGRSVTWGETRQDLPENPERFDSLPCVLGQEGFtSGRHYWEVE-VGD------------RT 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1835 EWsdesALG-CND---KSWGLFCSP-HGYYA--KHNNE-------PTDIPVpSSRSSRVGVYLDWPAGTLSFYSVfSDTl 1900
Cdd:cd15819     68 SW----DLGvCRDnvmRKGRVTLSPeNGFWAirLYGNEywaltspETPLTL-KEPPRRVGIFLDYEAGDVSFYNM-TDG- 140

                          170       180
                   ....*....|....*....|....*....
gi 2073512899 1901 THLHTF-HSTFTESLYPGFRVWPDSSVSL 1928
Cdd:cd15819    141 SHIYTFpQTAFSGPLRPFFRLWSSDSGPL 169
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 487-558 2.80e-31

Fish-specific NACHT associated domain; This domain is frequently found associated with the NACHT domain (pfam05729) in fish and other vertebrates.


Pssm-ID: 464185 [Multi-domain]  Cd Length: 72  Bit Score: 117.71  E-value: 2.80e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2073512899  487 HKASMKRRFESISEGIIRSETQTLLNKIYTELYITEGESEGVNNEHEVWQVESASRSQTTEDTAINCNDIFK 558
Cdd:pfam14484    1 LKSNLKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAASKKPESEETPIRCEDIFK 72
SPRY_PRY_C-II cd13734
PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, ...
 1760-1922 9.11e-31

PRY/SPRY domain in tripartite motif-containing proteins 1, 9, 18, 36, 46, 67,76 (TRIM1, TRIM9, TRIM18, TRIM36, TRIM46, TRIM67, TRIM76); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several Class I TRIM proteins, including TRIM1, TRIM9, TRIM18, TRIM36, TRIM46, TRIM67 and TRIM76. TRIM1 (also known as MID2) and its close homolog, TRIM18 (also known as MID1), both contain a B30.2-like domain at their C-terminus and a single fibronectin type III (FN3) motif between it and their N-terminal RBCC domain. Their coiled-coil motifs mediate both homo- and heterodimerization, a prerequisite for association of the rapamycin-sensitive PP2A regulatory subunit Alpha 4 with microtubules. Mutations in TRIM18 have shown to cause Opitz syndrome, a disorder causing congenital anomalies such as cleft lip and palate as well as heart defects. TRIM9 is expressed mainly in the cerebral cortex, and functions as an E3 ubiquitin ligase. Its immunoreactivity is severely decreased in affected brain areas in Parkinson's disease and dementia with Lewy bodies, possibly playing an important role in the regulation of neuronal function and participating in pathological process of Lewy body disease through its ligase. TRIM36 interacts with centromere protein-H, one of the kinetochore proteins and possibly associates with chromosome segregation; an excess of TRIM36 may cause chromosomal instability. TRIM46 has not yet been characterized. TRIM67 negatively regulates Ras activity via degradation of 80K-H, leading to neural differentiation, including neuritogenesis. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It is possibly involved in protein kinase A signaling as well as vesicular trafficking. It has also been implicated in Duchenne muscular dystrophy and cardiac disease. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site.


Pssm-ID: 293969 [Multi-domain]  Cd Length: 166  Bit Score: 119.69  E-value: 9.11e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1760 TLDPNTAYRTLSLSEGNRKVTCVTKEQP--YPDHPERFDFWSQVLCREGL-SGRCYWEAEWSGDGA-EIAVAYKSIKRKE 1835
Cdd:cd13734      2 KLDPKTAHRKLRLSNDNLTVEYDPEGSKdqAAVLPRRFTGSPAVLGDVAIsSGRHYWEVSVSRSTSyRVGVAYKSAPRDE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1836 WsdesaLGCNDKSWGLFCSPHGYYAKHNNEPTDIPVPSsRSSRVGVYLDWPAGTLSFYSVfsDTLTHLHTFHSTFTESLY 1915
Cdd:cd13734     82 D-----LGKNSTSWCLSRDNNRYTARHDGKVVDLRVTG-HPARIGVLLDYDNGTLSFYDA--ESKQHLYTFHVDFEGPVC 153


                   ....*..
gi 2073512899 1916 PGFRVWP 1922
Cdd:cd13734    154 PAFAVWN 160
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 1340-1687 1.94e-30

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 124.00  E-value: 1.94e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1340 LKILRLKGCKLTHESCKVVASFLQSANPLLELDLSNNVLR--DSGVQLLSKGLSSPhCKLQTLRLTDCHISDDGyvCLAL 1417
Cdd:cd00116     25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGriPRGLQSLLQGLTKG-CGLQELDLSDNALGPDG--CGVL 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1418 TLMANPSCVKELDLSNNNSGESAKNLLFATLKDPHLKMEELRLAGCKLTERSYEIVASALqSANSPLRELDLGHSDLQQS 1497
Cdd:cd00116    102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKAL-RANRDLKELNLANNGIGDA 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1498 G-EMLLSALQSpNCKLETLRLTGCKLT---GRFLALTLQgANPHLRELDISDgelqysggellhqplnqdCKVRLICCRl 1573
Cdd:cd00116    181 GiRALAEGLKA-NCNLEVLDLNNNGLTdegASALAETLA-SLKSLEVLNLGD------------------NNLTDAGAA- 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1574 kdsscavmasvlqfcvsqlsvldmtgcdlqtsdeKLLSCLGNPNCQLKTLKLADCKLTEESCKALASTLQSSVSLTELDL 1653
Cdd:cd00116    240 ----------------------------------ALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDL 285

                          330       340       350
                   ....*....|....*....|....*....|....
gi 2073512899 1654 TNSELKDSGIQLLSAGLSNPHCKLQTLRLSGCLI 1687
Cdd:cd00116    286 RGNKFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 1437-1736 2.03e-29

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 120.92  E-value: 2.03e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1437 GESAKNLLFATLKDPHLKMEELRLAGCKLTERSYEIVASALQsANSPLRELDLGHSDLQQSGEMLLSALQS--PNCKLET 1514
Cdd:cd00116      7 GELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALR-PQPSLKELCLSLNETGRIPRGLQSLLQGltKGCGLQE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1515 LRLTGCKLTG---RFLALTLQgaNPHLRELDISDGELQYSGGELLHQPLnQDCKVRL---IC--CRLKDSSCAVMASVLQ 1586
Cdd:cd00116     86 LDLSDNALGPdgcGVLESLLR--SSSLQELKLNNNGLGDRGLRLLAKGL-KDLPPALeklVLgrNRLEGASCEALAKALR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1587 FcVSQLSVLDMTGCDLQTSDEKLLsCLGNP-NCQLKTLKLADCKLTEESCKALASTLQSSVSLTELDLTNSELKDSGIQL 1665
Cdd:cd00116    163 A-NRDLKELNLANNGIGDAGIRAL-AEGLKaNCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAA 240

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2073512899 1666 LSAGLSNPHCKLQTLRLSGCLITHQGCSFLASALKSNPfYLKQLDLSYNHPGDSGVRELTDRLNDPNCKLE 1736
Cdd:cd00116    241 LASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKE-SLLELDLRGNKFGEEGAQLLAESLLEPGNELE 310
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 568-736 1.60e-28

NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 113.55  E-value: 1.60e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  568 RTAMTKGIAGIGKTVSVQKFILDWAEEKANQDVDFMFILPFRVLNLVKhDQYSLHKLLLDFHPELRELQDGEYKDRC--- 644
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQGFDFVFFLPCRELSRSG-NARSLADLLFSQWPEPAAPVSEVWAVILelp 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  645 --IVFIFDGLDESRlplnfqenQQLSDVTQTSSVDVLMTSLIQGSLLPSAHIWITSRPAAASQIPSQ-CINQVTEVRGFS 721
Cdd:pfam05729   80 erLLLILDGLDELV--------SDLGQLDGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGlEEPRYLEVRGFS 151

                          170
                   ....*....|....*
gi 2073512899  722 DPQKEEYFRKRISDQ 736
Cdd:pfam05729  152 ESDRKQYVRKYFSDE 166
SPRY_PRY_TRIM35 cd12893
PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is ...
 1760-1929 1.60e-28

PRY/SPRY domain in tripartite motif-containing protein 35 (TRIM35); This PRY/SPRY domain is found at the C-terminus of the overall domain architecture of tripartite motif 35, TRIM35 (also known as hemopoietic lineage switch protein), which includes a RING finger domain (RING) and a B-box motif (BBOX). TRIM35 may play a role as a tumor suppressor and is implicated in the cell death mechanism.


Pssm-ID: 293950 [Multi-domain]  Cd Length: 171  Bit Score: 113.50  E-value: 1.60e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1760 TLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL-SGRCYWEAEwSGDGAE--IAVAYKSIKRKEW 1836
Cdd:cd12893      3 TLDPNTAHPWLSLSEDLTSVRYSSEKQQLPDNPERFDPYPCVLGSEGFtSGKHSWDVE-VGDNTSwmLGVAKESVQRKGK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1837 -SDESALGCndksWGLFCSPHGYYAKHNNEPTDIPVPSSRSSRVGVYLDWPAGTLSFYSvfSDTLTHLHTFHSTFTESLY 1915
Cdd:cd12893     82 fTLSPESGF----WTIGFSEGKYSARTSPEPRTPLRVKQKPQRIRVQLDWDRGKVSFSD--PDTNTHIHTFTHTFTERVF 155

                          170
                   ....*....|....*
gi 2073512899 1916 PGFRVW-PDSSVSLC 1929
Cdd:cd12893    156 PYFYTGcKSEPLRIL 170
SPRY_PRY_TRIM25 cd13736
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25); This domain, consisting of ...
 1759-1929 1.18e-27

PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM25 proteins (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function.


Pssm-ID: 293971 [Multi-domain]  Cd Length: 169  Bit Score: 111.13  E-value: 1.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1759 LTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGLS-GRCYWEAEWSGDG-AEIAVAYKSIKRKew 1836
Cdd:cd13736      1 VIFDYNTAHNKVSLSENYTKASVSDDPQNYREHPQRFTYCSQVLGLHCFKqGIHYWEVELQKNNfCGVGICYGSMDRQ-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1837 SDESALGCNDKSWGLFCSPHGYYAKHNNEPTDIpvPSSRSSRVGVYLDWPAGTLSFYSVfSDTLTHLHTFHSTFTESLYP 1916
Cdd:cd13736     79 GPESRLGRNSESWCVEWFNVKISAWHNNVEKTL--PSTKATRVGVLLNCDHGFVIFFAV-QDKVHLMYKFKVDFTEALYP 155

                          170
                   ....*....|....
gi 2073512899 1917 GFRVWPD-SSVSLC 1929
Cdd:cd13736    156 AFWVFSAgTTLSLC 169
SPRY_PRY_TRIM15 cd15826
PRY/SPRY domain in tripartite motif-binding protein 15 (TRIM15); This domain, consisting of ...
 1759-1928 2.77e-26

PRY/SPRY domain in tripartite motif-binding protein 15 (TRIM15); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of tripartite motif-containing protein 15 (TRIM15), also referred to as RING finger protein 93 (RNF93) or Zinc finger protein B7 or 178 (ZNFB7 or ZNF178). TRIM15 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. The PRY and SPRY/B30.2 domains can function as immune defense components and in pathogen sensing. TRIM15 has been shown to regulate inflammatory and innate immune signaling, in addition to displaying antiviral activities. Down-regulation of TRIM15, as well as TRIM11, enhances virus release, suggesting that these proteins contribute to the endogenous restriction of retroviruses in cells. TRIM15 is also a regulatory component of focal adhesion turnover and cell migration.


Pssm-ID: 293998 [Multi-domain]  Cd Length: 170  Bit Score: 107.26  E-value: 2.77e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1759 LTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGLS-GRCYWEAEW---SGDGAEIAVAYKSIKRK 1834
Cdd:cd15826      2 VTLDPQTASGSLVLSEDRKSVRYTRQKQNLPDSPLRFDGLPAVLGSPGFSsGRHRWQVEVqlgDGGGCTVGVAGESVRRK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1835 ewsDESALGCNDKSWGLFCSPHGYYAkhNNEP-TDIPvPSSRSSRVGVYLDWPAGTLSFYSvfSDTLTHLHTFHSTFTES 1913
Cdd:cd15826     82 ---GEMGLSAEDGVWAVILSHQQCWA--STSPgTDLP-LSEIPRRVGVALDYEAGTVTLTN--AETQEPIFTFTASFSGK 153

                          170
                   ....*....|....*.
gi 2073512899 1914 LYPGFRVW-PDSSVSL 1928
Cdd:cd15826    154 VFPFFAVWkKGSRLTL 169
SPRY_PRY_TRIM41 cd13741
PRY/SPRY domain in tripartite motif-binding protein 41 (TRIM41); This domain, consisting of ...
 1758-1929 4.01e-26

PRY/SPRY domain in tripartite motif-binding protein 41 (TRIM41); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of tripartite motif-containing protein 41 (TRIM41). TRIM41 (also known as RING finger-interacting protein with C kinase or RINCK) is localized to speckles in the cytoplasm and nucleus, and functions as an E3 ligase that catalyzes the ubiquitin-mediated degradation of protein kinase C.


Pssm-ID: 240499 [Multi-domain]  Cd Length: 199  Bit Score: 107.93  E-value: 4.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1758 ELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL-SGRCYWEAEWSG-DGAEIAVAYKSIKRKE 1835
Cdd:cd13741      1 DLTLDPDTAHPALLLSPDRRGVRLAERRQEVPEHPKRFSADCCVLGAQGFrSGRHYWEVEVGGrRGWAVGAARESTHHKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1836 --WSDESALGCNDKSWG----------LFCSPH-------------GYYAKHNNEPTDIPvPSSRSSRVGVYLDWPAGTL 1890
Cdd:cd13741     81 kvGSGGSSVSSGDASSSrhhhrrrrlhLPQQPLlqrevwcvgtngkRYQAQSSTEQTLLS-PSEKPRRFGVYLDYEAGRL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2073512899 1891 SFYSvfSDTLTHLHTFHSTF-TESLYPGFRVWPDSS-VSLC 1929
Cdd:cd13741    160 GFYN--AETLAHVHTFSAAFlGERVFPFFRVLSKGTrIKLC 198
SPRY_PRY_TRIM69 cd15818
PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger ...
 1759-1918 4.16e-26

PRY/SPRY domain in tripartite motif-binding protein 69 (TRIM69), also known as RING finger protein 36 (RNF36); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM69, which is also known as RING finger protein 36 (RNF36) or testis-specific ring finger (Trif). TRIM69 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. The mouse ortholog of this gene is specifically expressed in germ cells at the round spermatid stages during spermatogenesis and, when overexpressed, induces apoptosis. TRIM69 has been shown to be a novel regulator of mitotic spindle assembly in tumor cells; it associates with spindle poles and promotes centrosomal clustering, and is therefore essential for formation of a bipolar spindle.


Pssm-ID: 293990 [Multi-domain]  Cd Length: 187  Bit Score: 107.20  E-value: 4.16e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1759 LTLDPNTAYRTLSLSEGnrkVTCV----TKeQPYPDHPERFDFWSQVLCREGL-SGRCYWEAE------WSgdgaeIAVA 1827
Cdd:cd15818     15 ITLDPKTAHPNLILSED---LTCVwhgdTK-QMLPDNPERFDSSVAVLGSEGFtSGKHYWEVEvakktkWT-----LGVV 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1828 YKSIKRKewsdesalGCNDkswglfCSP-HGYY---AKHNNEPTDIPVPS------SRSSRVGVYLDWPAGTLSFYSVfs 1897
Cdd:cd15818     86 RESINRK--------GNCP------LSPeDGFWllrLRNQNELKALDVPSfsltltSNLNKVGIYLDYEGGQVSFYNA-- 149

                          170       180
                   ....*....|....*....|.
gi 2073512899 1898 DTLTHLHTFHSTFTESLYPGF 1918
Cdd:cd15818    150 NTMSHIYTFSDTFTEKIYPYF 170
SPRY_BSPRY cd12904
SPRY domain in Ro-Ret family; This domain, named BSPRY, has been identified in the Ro-Ret ...
 1759-1928 1.95e-25

SPRY domain in Ro-Ret family; This domain, named BSPRY, has been identified in the Ro-Ret family, since the protein is composed of a B-box, an alpha-helical coiled coil and a SPRY domain. The gene for BSPRY resides on human chromosome 9 and is specifically expressed in testis. The function of BSPRY is not known, but several related proteins of the RING-Box-coiled-coil (RBCC) family have been implicated in cell transformation.


Pssm-ID: 293961 [Multi-domain]  Cd Length: 171  Bit Score: 104.81  E-value: 1.95e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1759 LTLDPNTAYRTLSLSEGNRKVTCVTK--EQPYPDHPERFDFWSQVLCREGL-SGRCYWEAEWSGDGA-EIAVAYKSIKRK 1834
Cdd:cd12904      1 LRFDERTVSPLLSLSEDRRTLTFSPKkaRQSPPDDPERFDHWPNALASLSFsSGTHAWVVDVGKSCAyKVGVCYGSLERK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1835 EWSDESALGCNDKSWGL--------FCsphgyyakHNNEPTDIPVpSSRSSRVGVYLDWPAGTLSFYSvfSDTLTHLHTF 1906
Cdd:cd12904     81 GSGNEARLGYNAFSWVFsrydgefsFS--------HNGQHVPLEL-LKCPARVGVLLDWPSQELLFYD--PDSCTVLHSH 149

                          170       180
                   ....*....|....*....|..
gi 2073512899 1907 HSTFTESLYPGFRVwPDSSVSL 1928
Cdd:cd12904    150 REAFAAPLLPVFAV-ADQSISI 170
SPRY_PRY_RNF135 cd12902
PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct ...
 1759-1918 9.65e-25

PRY/SPRY domain in RING finger protein RNF135; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of the RING finger protein RNF135 (also known as Riplet/RNF135), which ubiquitinates RIG-I (retinoic acid-inducible gene-I) to promote interferon-beta induction during the early phase of viral infection. Normally, RIG-I is activated by TRIM25 in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. However, RNF135, consisting of an N-terminal RING finger domain, C-terminal SPRY and PRY motifs and showing sequence similarity to TRIM25, acts as an alternative factor that promotes RIG-I activation independent of TRIM25.


Pssm-ID: 293959 [Multi-domain]  Cd Length: 168  Bit Score: 102.59  E-value: 9.65e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1759 LTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFwSQVLCREGLS-GRCYWEAEWS-GDGAEIAVAYKSIKRKEW 1836
Cdd:cd12902      1 PTFDLRSLSCSLEVSEDSRKVTVSHGPQAYAWSPDRFSI-SQVLCSQAFSsGQHYWEVDTRqCSHWAVGVASWEMSRDQM 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1837 sdesaLGCNDKSWGL-FCSPHGYYAKHNNEPTDIpvPSSRSSRVGVYLDWPAGTLSFYSVfSDTLTHLHTFHSTFTESLY 1915
Cdd:cd12902     80 -----LGRTMDSWCIeWKGTGQLSAWHMNKETVL--GSDKPRVVGIWLDLEEGKLAFYSV-ANQERLLHECEVSASSPLH 151


                   ...
gi 2073512899 1916 PGF 1918
Cdd:cd12902    152 PAF 154
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 1048-1460 8.96e-24

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 104.36  E-value: 8.96e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1048 DEFDLKKYKTSPEGRRRLVPAVRCCRKALLADCKLSERSFEIVASALQsANSPLRELDLSHSDLQQSGEMLGSALQspnc 1127
Cdd:cd00116      1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALR-PQPSLKELCLSLNETGRIPRGLQSLLQ---- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1128 kletlrlagckltgrflALTlqgANPHLRELDISDGELQDCGgellhkplnedckvrlkhssCAVVASVLQfcVSQLSVL 1207
Cdd:cd00116     76 -----------------GLT---KGCGLQELDLSDNALGPDG--------------------CGVLESLLR--SSSLQEL 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1208 DMSGCDLQTSEEK-LPSSLGNPNCRLKTLRLAGCKLTGRF---LALTLQgANPHLRELDISDSELQDCGgellhqplnqe 1283
Cdd:cd00116    114 KLNNNGLGDRGLRlLAKGLKDLPPALEKLVLGRNRLEGASceaLAKALR-ANRDLKELNLANNGIGDAG----------- 181

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1284 ckVRLLCCRLKHsscavvasvlqfcvsqlsdldmsgcdpqtsvekllsslgnpNCRLKILRLKGCKLTHESCKVVASFLQ 1363
Cdd:cd00116    182 --IRALAEGLKA-----------------------------------------NCNLEVLDLNNNGLTDEGASALAETLA 218

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1364 SANPLLELDLSNNVLRDSGVQLLSKGLSSPHCKLQTLRLTDCHISDDGYVCLAlTLMANPSCVKELDLSNNNSGESAKNL 1443
Cdd:cd00116    219 SLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLA-EVLAEKESLLELDLRGNKFGEEGAQL 297

                          410
                   ....*....|....*..
gi 2073512899 1444 LFATLKDPHLKMEELRL 1460
Cdd:cd00116    298 LAESLLEPGNELESLWV 314
SPRY_PRY_TRIM75 cd15829
PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75); This domain, consisting of ...
 1753-1924 4.54e-23

PRY/SPRY domain of tripartite motif-binding protein 75 (TRIM75); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM75, also known as Gm794. TRIM75 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM75 has a single site of positive selection in its RING domain associated with E3 ubiquitin ligase activity. It has not been detectably expressed experimentally due to their constant turnover by the proteasome, and therefore not been characterized.


Pssm-ID: 294001  Cd Length: 187  Bit Score: 98.52  E-value: 4.54e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1753 RKYACELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL-SGRCYWEAEwSGDGAEIAV----A 1827
Cdd:cd15829     15 KKFRVDVTLDPETAHPNLLVSEDKKCVTFTKKKQRVPDSPKRFTVNPVVLGFPGFhSGRHFWEVE-VGDKPEWAVgvckD 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1828 YKSIKRKEWSdESALGCndksWGLFCSPHGYYAkhnnePTDIPVPS---SRSSRVGVYLDWPAGTLSFYSVfsDTLTHLH 1904
Cdd:cd15829     94 SLSTKARRPP-SGQQGC----WRIQLQGGDYDA-----PGAVPPPLlleVKPRGIGVFLDYELGEISFYNM--PEKSHIH 161

                          170       180
                   ....*....|....*....|
gi 2073512899 1905 TFHSTFTESLYPGFRVWPDS 1924
Cdd:cd15829    162 TFTDTFSGPLRPYFYVGPDS 181
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
456-912 3.86e-22

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 104.50  E-value: 3.86e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  456 VLEGSKHLQTEHAPVKRAKLRDDILNRALVNHKASMKRRFESISegIIRSETQTLLNKIYTELYITEGESEGVNNEHEVW 535
Cdd:COG5635     66 ALSAAALLARALSALLLVLLLLESLLLLLLLLLLLAEALLALLE--LAALLKAVLLSLSGGSDLVLLLSESDLLLALLIL 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  536 QVESASRSQTTEDTAINCNDIFKSLPGQQRPIRTAMTK-----GIAGIGKTVSVQKFILDWAEEKANQDVDFMFILPFR- 609
Cdd:COG5635    144 LLDADGLLVSLDDLYVPLNLLERIESLKRLELLEAKKKrllilGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRd 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  610 ------VLNLVKHdqySLHKLLLDFHPELRELQDgeyKDRCiVFIFDGLDESRLPLNFQEN-QQLSDVTQTssvdvlmts 682
Cdd:COG5635    224 laeeasLEDLLAE---ALEKRGGEPEDALERLLR---NGRL-LLLLDGLDEVPDEADRDEVlNQLRRFLER--------- 287

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  683 liqgslLPSAHIWITSRPAAAsqiPSQCINQVTEVR--GFSDPQKEEYFRKRI-SDQNQANRIISHIKASRSLYIMCHMP 759
Cdd:COG5635    288 ------YPKARVIITSRPEGY---DSSELEGFEVLElaPLSDEQIEEFLKKWFeATERKAERLLEALEENPELRELARNP 358

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  760 VFCWISATVLQqileedDGKEPPKTLTEMFIHFL--LIQTTRKKQKYQEENDIERQRLLEshkdvilKLAELAFKHLENG 837
Cdd:COG5635    359 LLLTLLALLLR------ERGELPDTRAELYEQFVelLLERWDEQRGLTIYRELSREELRE-------LLSELALAMQENG 425

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2073512899  838 NLMFYEEDLKECGIDVSEASVYSG-MCTEIFREECVFHHK--KVYCFVHLSIQEFLAALHVFASYLSKNMKALTPFLK 912
Cdd:COG5635    426 RTEFAREELEEILREYLGRRKDAEaLLDELLLRTGLLVERgeGRYSFAHRSFQEYLAARALVEELDEELLELLAEHLE 503
SPRY_PRY_TRIM60_75 cd15817
PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75); This domain, ...
 1758-1929 5.68e-22

PRY/SPRY domain of tripartite motif-binding protein 60 and 75 (TRIM60 and TRIM75); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM60 and TRIM75, both composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM60 domain is also known as RING finger protein 33 (RNF33) or 129 (RNF129). Based on its expression profile, RNF33 likely plays an important role in the spermatogenesis process, the development of the pre-implantation embryo, and in testicular functions; Rnf33 is temporally transcribed in the unfertilized egg and the pre-implantation embryo, and is permanently silenced before the blastocyst stage. Mice experiments have shown that RNF33 associates with the cytoplasmic motor proteins, kinesin-2 family members 3A (KIF3A) and 3B (KIF3B), suggesting possible contribution to cargo movement along the microtubule in the expressed sites. TRIM75, also known as Gm794, has a single site of positive selection in its RING domain associated with E3 ubiquitin ligase activity. It has not been detectably expressed experimentally due to their constant turnover by the proteasome, and therefore not been characterized.


Pssm-ID: 293989 [Multi-domain]  Cd Length: 168  Bit Score: 94.54  E-value: 5.68e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1758 ELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL-SGRCYWEAEWSGDGAEIAVAYKSIKRKEW 1836
Cdd:cd15817      1 DLILDPETAHPNLIVSEDRKAVRYRRMKPNCPYDPRRFTVYPAVLGSEGFdSGRHFWEVEVGGKGEWILGVCKDSLPRNA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1837 SDESALgcNDKSWGLFCSPHGYYAKhNNEPTDIpVPSSRSSRVGVYLDWPAGTLSFYSVFSDtlTHLHTFHSTFTESLYP 1916
Cdd:cd15817     81 QDPPSP--LGGCWQIGRYMSGYVAS-GPKTTQL-LPVVKPSRIGIFLDYELGEVSFYNMNDR--SHLYTFTDTFTGKLIP 154

                          170
                   ....*....|....
gi 2073512899 1917 GFRVWPDS-SVSLC 1929
Cdd:cd15817    155 YFYVGPDSePLTIC 168
SPRY_PRY_TRIM60 cd15828
PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger ...
 1758-1924 1.36e-21

PRY/SPRY domain of tripartite motif-binding protein 60 (TRIM60) also known as RING finger protein 33 (RNF33); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM60, which is also known as RING finger protein 33 (RNF33) or 129 (RNF129). TRIM60 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. Based on its expression profile, RNF33 likely plays an important role in the spermatogenesis process, the development of the pre-implantation embryo, and in testicular functions; Rnf33 is temporally transcribed in the unfertilized egg and the pre-implantation embryo, and is permanently silenced before the blastocyst stage. Mice experiments have shown that RNF33 associates with the cytoplasmic motor proteins, kinesin-2 family members 3A (KIF3A) and 3B (KIF3B), suggesting possible contribution to cargo movement along the microtubule in the expressed sites.


Pssm-ID: 294000 [Multi-domain]  Cd Length: 180  Bit Score: 93.89  E-value: 1.36e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1758 ELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL-SGRCYWEAEwSGDGAE--IAVAYKSIKRK 1834
Cdd:cd15828     11 DVTLDPETAHPQLTVSEDRKSVLYGEMKQNVCYNPRRFYLCPAVLGSEGFhSGRQYWEVE-VGDKPEwtLGVCQDCLPRN 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1835 eWSDESALgcNDKSWGLFCSPHGYYAKHNNEPTDIpVPSSRSSRVGVYLDWPAGTLSFYSVFSDTLthLHTFHSTFTESL 1914
Cdd:cd15828     90 -WSNQPSV--QDGLWAIGRYSESNYVALGPKKIQL-LPKVRPSKIGIFLDYELGEVSFYNMNDRSL--LYTFSDSFTGTL 163

                          170
                   ....*....|
gi 2073512899 1915 YPGFRVWPDS 1924
Cdd:cd15828    164 WPYFYTGTDS 173
PRY pfam13765
SPRY-associated domain; PRY is a 50-60 amino acids domain associated with SPRY domains, ...
 1759-1807 2.87e-21

SPRY-associated domain; PRY is a 50-60 amino acids domain associated with SPRY domains, adjacent to its N-terminal. PRY and SPRY domains are structurally very similar and consist of a beta sandwich fold. Distant homologs are domains in butyrophilin/marenostrin/pyrin, evolutionarily more ancient than SPRY/B30.2 counterpart.


Pssm-ID: 463976  Cd Length: 49  Bit Score: 88.30  E-value: 2.87e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2073512899 1759 LTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL 1807
Cdd:pfam13765    1 VTLDPNTAHPSLVLSEDLKSVRYGDERQNVPDNPERFDSWPCVLGSEGF 49
SPRY_PRY_BTN3 cd15820
PRY/SPRY domain of butyrophilin 3 (BTN3), includes BTN3A1, BTN3A2, BTN3A3 as well as BTN-like ...
 1756-1929 3.10e-21

PRY/SPRY domain of butyrophilin 3 (BTN3), includes BTN3A1, BTN3A2, BTN3A3 as well as BTN-like 3 (BTNL3); BTN3A also known as CD277; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of butyrophilin family 3A (BTN3A); duplication events have led to three paralogs in primates: BTN3A1, BTN3A2, and BTN3A3. BTNs belong to receptor glycoproteins of immunoglobulin (Ig) superfamily, characterized by the presence of extracellular Ig-like domains (IgV and/or IgC). BTN3 transcripts are ubiquitously present in all immune cells (T cells, B cells, NK cells, monocytes, dendritic cells, and hematopoietic precursors) with different expression levels; BTN3A1 and BTN3A2 are expressed mainly by CD4+ and CD8+ T cells, BTN3A2 is the major form expressed in NK cells, and BTN3A3 is poorly expressed in these immune cells. The PRY/SPRY domain of the BTN3A1 isoform mediates phosphoantigen (pAg)-induced activation by binding directly to the pAg.


Pssm-ID: 293992 [Multi-domain]  Cd Length: 176  Bit Score: 92.88  E-value: 3.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1756 ACELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVL-CREGLSGRCYWEAEwSGDGAE--IAVAYKSIK 1832
Cdd:cd15820      3 PADVILDPDTANPILLISEDQRSLQWADEPQNLPDNPKRFDWHYCVLgCKSFTSGRHFWEVE-VGDRKEwyVGVCRENVE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1833 RKEWSDESAlgcNDKSWGLFCSPHGYYAKHNNEPTDIPVPSSrSSRVGVYLDWPAGTLSFYSVFSDtlTHLHTF-HSTFT 1911
Cdd:cd15820     82 RKLWVKMAP---ENGFWTIGLSDGNDYQALTDPRTKLTIANP-PQRVGVFLDYETGEVSFYNAMDG--SHIYTFpHTSFS 155

                          170       180
                   ....*....|....*....|
gi 2073512899 1912 ESLYPGFRV--WPDSSVSLC 1929
Cdd:cd15820    156 GPLYPVFRLlsWDPTALTIC 175
SPRY_PRY_TRIM7 cd13740
PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); This domain, consisting of the ...
 1758-1922 3.98e-21

PRY/SPRY domain in tripartite motif-binding protein 7 (TRIM7); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of tripartite motif-containing protein 7 (TRIM7), also referred to as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90). TRIM7 or GNIP interacts with glycogenin and stimulates its self-glucosylating activity via its SPRY domain. The GNIP gene encodes at least four distinct isoforms of GNIP, of which three (GNIP1, GNIP2, and GNIP3) have the B30.2 domain.


Pssm-ID: 293975 [Multi-domain]  Cd Length: 169  Bit Score: 92.33  E-value: 3.98e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1758 ELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL-SGRCYWEAE-WSGDGAEIAVAYKSIKRK- 1834
Cdd:cd13740      1 ELTLDPDSANPRLILSLDLKSVRLGERAQDLPNHPCRFDTNTRVLASCGFsSGRHHWEVEvGSKDGWAFGVARESVRRKg 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1835 --EWSDESALgcndksWGLFCSPHGYYAKHNNEPTdiPVPSSRSSRVGVYLDWPAGTLSFYSVfsDTLTHLHTFHSTFTE 1912
Cdd:cd13740     81 ltPFTPEEGV------WALQLNGGQYWAVTSPERT--PLSCGHLSRVRVALDLEVGAVSFYAA--EDMRHIYTFRVNFQE 150

                          170
                   ....*....|....*....
gi 2073512899 1913 SLYPGF---------RVWP 1922
Cdd:cd13740    151 RVFPLFsvcstgtylRIWP 169
SPRY smart00449
Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are ...
 1808-1931 7.74e-21

Domain in SPla and the RYanodine Receptor; Domain of unknown function. Distant homologues are domains in butyrophilin/marenostrin/pyrin homologues.


Pssm-ID: 214669  Cd Length: 122  Bit Score: 89.66  E-value: 7.74e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  1808 SGRCYWEAEWSGDGA-EIAVAYKSIKRKewsDESALGCNDKSWGLF-CSPHGYyakHNNEPTDIPVPSSRS-SRVGVYLD 1884
Cdd:smart00449    1 SGRHYFEVEIGDGGHwRVGVATKSVPRG---YFALLGEDKGSWGYDgDGGKKY---HNSTGPEYGLPLQEPgDVIGCFLD 74

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 2073512899  1885 WPAGTLSFYSVfSDTLTHLHTFHSTFTESLYPGFRVWPDSS--VSLCQI 1931
Cdd:smart00449   75 LEAGTISFYKN-GKYLHGLAFFDVKFSGPLYPAFSLGSGNSvrLNFGPL 122
SPRY_PRY_TRIM18 cd12892
PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59; This domain, consisting of the ...
 1761-1921 1.58e-20

PRY/SPRY domain of TRIM18/MID1, also known as FXY or RNF59; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is at the C-terminus of the overall domain architecture of MID1 (also known as FXY, RNF59, TRIM18) gene represented by a RING finger domain (RING), two B-box motifs (BBOX), coiled-coil C-terminal to Bbox domain (BBC) and fibronectin type 3 domain (FN3). Mutations in the human MID1 gene result in X-linked Opitz G/BBB syndrome (OS), a disorder affecting development of midline structures, causing craniofacial, urogenital, gastrointestinal and cardiovascular abnormalities. A unique MID1 gene mutation located in a variable loop in the SPRY domain alters conformation of the binding pocket and may affect the binding affinity to the PRY/SPRY domain.


Pssm-ID: 240472  Cd Length: 177  Bit Score: 90.84  E-value: 1.58e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1761 LDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL---SGRCYWEAEWSGDG-AEIAVAYKSIKRKEW 1836
Cdd:cd12892      4 LDPKSAHRKLKVSHDNLTVERDETSSKKSHTPERFTSQGSYGVAGNVfidSGRHYWEVVISGSTwYAIGIAYKSAPKHEW 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1837 sdesaLGCNDKSWGLFCSPHGYYAKHNNEptDIPV-PSSRSSRVGVYLDWPAGTLSFYSVFSDtlTHLHTFHSTFTESLY 1915
Cdd:cd12892     84 -----IGKNSASWVLCRCNNNWVVRHNSK--EIPIePSPHLRRVGILLDYDNGSLSFYDALNS--IHLYTFDIAFAQPVC 154


                   ....*.
gi 2073512899 1916 PGFRVW 1921
Cdd:cd12892    155 PTFTVW 160
SPRY_PRY_TRIM11 cd15811
PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger ...
 1758-1930 4.83e-20

PRY/SPRY domain of tripartite motif-binding protein 11 (TRIM11), also known as RING finger protein 92 (RNF92); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM11, also known as RING finger protein 92 (RNF92) or BIA1. TRIM11 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It localizes to the nucleus and the cytoplasm; it is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 increases expression of dopamine beta-hydroxylase gene by interacting with the homeodomain transcription factor, PHOX2B, via the B30.2/SPRY domain, thus playing a potential role in the specification of noradrenergic (NA) neuron phenotype. It has also been shown that TRIM11 plays a critical role in the clearance of mutant PHOX2B, which causes congenital central hypoventilation syndrome, via the proteasome. TRIM11 binds a key component of the activator-mediated cofactor complex (ARC105), and destabilizes it, through the ubiquitin-proteasome system; ARC105 mediates chromatin-directed transcription activation and is a key regulatory factor for transforming growth factor beta (TGFbeta) signaling.


Pssm-ID: 293983 [Multi-domain]  Cd Length: 169  Bit Score: 89.25  E-value: 4.83e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1758 ELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL-SGRCYWEAEwSGDGAEIA--VAYKSIKRK 1834
Cdd:cd15811      1 DVTLDPDTANPELVLSEDRRSVRRGDLRQALPDSPERFDPGPCVLGRERFtSGRHYWEVE-VGDRTSWAlgVCKENVNRK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1835 EWSDESAlgcNDKSWGLFcsphgYYAKHNNEPTDIPVP-SSRSSRVGVYLDWPAGTLSFYSVFSDTLthLHTFHST-FTE 1912
Cdd:cd15811     80 EKGELSA---GNGFWILV-----FLGNYYSSERRTFAPlRDPPRRVGIFLDYEAGHLSFYSATDGSL--LFIFPETpFSG 149

                          170       180
                   ....*....|....*....|..
gi 2073512899 1913 SLYPGFRvwPDSS----VSLCQ 1930
Cdd:cd15811    150 TLRPLFS--PLSSsptpMTICR 169
SPRY_PRY_TRIM50_72 cd12897
PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72; This domain, ...
 1758-1923 1.05e-19

PRY/SPRY domain in tripartite motif-binding (TRIM) proteins TRIM50 and TRIM72; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of several TRIM proteins, including TRIM72 and TRIM50. TRIM72 (also known as MG53) has been shown to perform a critical function in membrane repair following acute muscle injury by nucleating the assembly of the repair machinery at injury sites. It is expressed specifically in skeletal muscle and heart, and tethered to the plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23.


Pssm-ID: 293954  Cd Length: 191  Bit Score: 88.82  E-value: 1.05e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1758 ELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGLS-GRCYWEAEwSGDGAEIAVAyksIKRKEW 1836
Cdd:cd12897     13 SLTFDPATAHPLLVVSSGGTVVECGLQKQRRASQPERFDKSTCVVASQGFSeGEHYWEVV-VGDKPRWALG---VIKGTA 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1837 SDESALGCNDKS--WGLFCSPHGYYAKHN--NEPTDIPVPSsRSSRVGVYLDWPAGTLSFY-SVFSDTLTHLHTFHSTFT 1911
Cdd:cd12897     89 SRKGKLHASPSHgvWLIGLKEGKVYEAHGepKEPRPLRVAG-RPHRIGVYLSFEDGVLSFFdASDPDDLRTLYTFQERFQ 167

                          170
                   ....*....|...
gi 2073512899 1912 ESLYPGFRV-WPD 1923
Cdd:cd12897    168 GKLYPFFDVcWHD 180
PRY smart00589
associated with SPRY domains;
1756-1807 4.11e-19

associated with SPRY domains;


Pssm-ID: 128857  Cd Length: 52  Bit Score: 82.24  E-value: 4.11e-19
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2073512899  1756 ACELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL 1807
Cdd:smart00589    1 AVDVTLDPDTAHPYLLLSEDRRSVRYGDLKQSLPDNPERFDSYPCVLGSQGF 52
SPRY_PRY_TRIM38 cd15815
PRY/SPRY domain of tripartite motif-binding protein 38 (TRIM38), also known as Ring finger ...
 1753-1924 6.11e-19

PRY/SPRY domain of tripartite motif-binding protein 38 (TRIM38), also known as Ring finger protein 15 (RNF15); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM38, which is also known as RING finger protein 15 (RNF15) or RORET. TRIM38 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. TRIM38 has been shown to act as a suppressor in TOLL-like receptor (TLR)-mediated interferon (IFN)-beta induction by promoting degradation of TRAF6 and NAP1 through the ubiquitin-proteasome system. Another study has shown that TRIM38 may act as a novel negative regulator for TLR3-mediated IFN-beta signaling by targeting TRIF for degradation. TRIM38 has been identified as a critical negative regulator in TNFalpha- and IL-1beta-triggered activation of NF-kappaB and MAP Kinases (MAPKs); it causes degradation of two essential cellular components, TGFbeta-associated kinase 1 (TAK1)-associating chaperones 2 and 3 (TAB2/3). The degradation is promoted through a lysosomal-dependent pathway, which requires the C-terminal PRY-SPRY of TRIM38. Enterovirus 71 infection induces degradation of TRIM38, suggesting that TRIM38 may play a role in viral infections.


Pssm-ID: 293987 [Multi-domain]  Cd Length: 182  Bit Score: 86.25  E-value: 6.11e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1753 RKYACELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL-SGRCYWEAE-WSGDGAEIAVAYKS 1830
Cdd:cd15815      9 RRHQVSVTLDPDTAHPELTLSKDQRQVTYGRCQENLDASPKRFTVLPCVLGCEGFtSGRHYFEVDvGEGTGWDVGVCLEN 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1831 IKRK-EWSDESALGcndkSWGL-FCSPHGYYAKhNNEPTDIPVpSSRSSRVGVYLDWPAGTLSFYSVfsDTLTHLHTF-H 1907
Cdd:cd15815     89 VQRGfGMKQEPEFG----FWTIrLCEEDGYVAL-TSPPTPLPL-REKPLVVGVFLDYEAGLVSFYNM--TTGSHIFTFpK 160

                          170
                   ....*....|....*..
gi 2073512899 1908 STFTESLYPGFRVWPDS 1924
Cdd:cd15815    161 ASFSDTLRPYFQVYQYS 177
SPRY_PRY_RFPL cd15821
Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4; This domain, consisting of the ...
 1754-1918 3.89e-18

Ret finger protein-like (RFPL), includes RFP1, 2, 3, 4; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of RFPL protein family, which includes RFPL1, RFPL2, RFPL3 and RFPL4. In humans, RFPL transcripts can be detected at the onset of neurogenesis in differentiating human embryonic stem cells, and in the developing human neocortex. The human RFPL1, 2, 3 genes have a role in neocortex development. RFPL1 is a primate-specific target gene of Pax6, a key transcription factor for pancreas, eye and neocortex development; human RFPL1 decreases cell number through its RFPL-defining motif (RDM) and SPRY domains. The RFPL4 (also known as RFPL4A) gene encodes a putative E3 ubiquitin-protein ligase expressed in adult germ cells and interacts with oocyte proteins of the ubiquitin-proteasome degradation pathway.


Pssm-ID: 293993 [Multi-domain]  Cd Length: 178  Bit Score: 83.90  E-value: 3.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1754 KYACELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL-SGRCYWEA------EWsgdgaEIAV 1826
Cdd:cd15821      1 KFQVDMTLDVDTANNYLIISEDLRSVRCGCFRQNRKELAERFDDALCVLGSPRFtSGRHYWEVdvgtstEW-----DLGV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1827 AYKSIKRKEwsdESALGCNDKSWGLFCSPHGYYAKHNNEPTDIPVpSSRSSRVGVYLDWPAGTLSFYSVfSDTlTHLHTF 1906
Cdd:cd15821     76 CRESVNRQG---PIELSPEHGFWTVSLRDGSVFFASTVPLTVLWV-NPRLHRVGIFLDMEMGTISFYDV-SDG-SHIFTF 149

                          170
                   ....*....|...
gi 2073512899 1907 HSTF-TESLYPGF 1918
Cdd:cd15821    150 TKISaEEPLRPFF 162
SPRY_PRY_TRIM58 cd15816
PRY/SPRY domain in tripartite motif-binding protein 58 (TRIM58), also known as BIA2; This ...
 1758-1920 1.36e-17

PRY/SPRY domain in tripartite motif-binding protein 58 (TRIM58), also known as BIA2; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM58, also known as BIA2. TRIM58 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins.It is implicated by genome-wide association studies (GWAS) to regulate erythrocyte traits, including cell size and number. Trim58 facilitates erythroblast enucleation by inducing proteolytic degradation of the microtubule motor dynein.


Pssm-ID: 293988 [Multi-domain]  Cd Length: 168  Bit Score: 82.15  E-value: 1.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1758 ELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL-SGRCYWEAEwSGDGAE--IAVAYKSIKRK 1834
Cdd:cd15816      1 DVKLDPATAHPSLLLTADLRSVQDGELWRDVPGNPERFDTWPCVLGLQSFsSGRHYWEVA-VGEKAEwgLGVCQDSAPRK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1835 ewsDESALGCNDKSWGLFCSPHGYYAKHNNePTDIPVPSSRSSRVGVYLDWPAGTLSFYSVFSDtlTHLHTFHSTFTESL 1914
Cdd:cd15816     80 ---GETTPSPENGVWAVWLLKGNEYMVLAS-PSVPLLQLRRPRRVGVFLDYEAGEISFYNVTAG--SHIYTFRQLFSGIL 153


                   ....*.
gi 2073512899 1915 YPGFRV 1920
Cdd:cd15816    154 RPYFFV 159
SPRY_PRY_TRIM20 cd15813
PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin; This ...
 1753-1918 2.04e-17

PRY/SPRY domain in tripartite motif-binding protein 20 (TRIM20), also known as pyrin; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM20, which is also known as pyrin or marenostrin. Unlike TRIM domains that are composed of RING/B-box/coiled-coil core, the N-terminal RING domain in TRIM20 is exchanged by a PYRIN domain (PYD), a prime mediator of protein interactions necessary for apoptosis, inflammation and innate immune signaling pathway, and it also harbors a C-terminal B30.2 domain. Mutations in pyrin (TRIM20) are associated with familial Mediterranean fever (FMF), a recessively hereditary periodic fever syndrome, characterized by episodes of inflammation and fever. These mutations cluster in the C-terminal B30.2 domain and therefore it is assumed that pyrin plays a role in the innate immune system by possibly effecting caspase-1-dependent IL-1beta maturation.


Pssm-ID: 293985  Cd Length: 184  Bit Score: 82.11  E-value: 2.04e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1753 RKYACELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVL-CREGLSGRCYWEAEWSGDGAEI-AVAYKS 1830
Cdd:cd15813      5 QAHAVNVTLDPETAHPNLIFSDDLKSVRLGNKWDRLPDNPERFDSCIIVLgSPSFTSGRHYWEVEVGDKTGWIlGVCKAS 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1831 IKRKewsDESALGCNDKSWGLFCSPHGYYAKHNNEPTD--IPVPssrSSRVGVYLDWPAGTLSFYSVfsDTLTHLHTF-H 1907
Cdd:cd15813     85 VSRK---GSMTLSPENGYWVVMMTKRNEYQASTSPPTRlwLREP---PRRVGIFLDYEAGDISFYNV--TAKSHIYTFtS 156

                          170
                   ....*....|.
gi 2073512899 1908 STFTESLYPGF 1918
Cdd:cd15813    157 FSSSGPLQPIF 167
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 10-79 2.21e-17

Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated speck-like protein containing a CARD) and similar proteins. ASC is an adaptor molecule that functions in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. ASC contains two domains from the Death Domain (DD) superfamily, an N-terminal pyrin-like domain and a C-terminal Caspase activation and recruitment domain (CARD). Through these 2 domains, ASC serves as an adaptor for inflammasome integrity and oligomerizes to form supramolecular assemblies. Included in this family is human PYNOD (also known as NLRP10 or NOD8) which via its Pyrin domain suppresses oligomerization of ASC, and ASC-mediated NF-kappaB activation. Other members of this subfamily are associated with ATPase domains and their function remains unknown. In general, Pyrin is a subfamily of the DD superfamily and functions in several signaling pathways. 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 CARD and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260033  Cd Length: 82  Bit Score: 78.33  E-value: 2.21e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2073512899   10 REVLRNTLDNLTGAEFKRFKHYLQDQGQ-----IAWGKLEKADTDDTVDLMVQVYST-GAGDIILSILKTIKHNQL 79
Cdd:cd08321      1 RDLLLDALEDLGEEELKKFKWKLRDIPLegyprIPRGKLENADRVDLVDLLVSYYGEdYAVEVTVEVLRAINQNDL 76
SPRY_PRY_TRIM50 cd13743
PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50); This domain, consisting of ...
 1747-1923 3.58e-17

PRY/SPRY domain in tripartite motif-binding protein 50 (TRIM50); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM50. TRIM50, an E3 ubiquitin ligase, is deleted in Williams-Beuren (WBS) syndrome, a multi-system neurodevelopmental disorder caused by the deletion of contiguous genes at chromosome region 7q11.23. It is specifically expressed in gastric parietal cells and may play an essential role in tubulovesicular dynamics. It also interacts with and increases the level of p62, a multifunctional adaptor protein that is implicated in various cellular processes such as the autophagy clearance of polyubiquitinated protein aggregates.


Pssm-ID: 293977  Cd Length: 189  Bit Score: 81.39  E-value: 3.58e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1747 RIKPGPRKyaceLTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGLS-GRCYWEaewsgdgaeIA 1825
Cdd:cd13743      6 KVLPAPEL----LKLDPLTAHPMLELSKGNTVVECGLLAQRLPSNPERFDYSNCVLASRGFSsGKHYWE---------VV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1826 VAYKSikrkEWSDESALGCNDKSWGLFCSPHG-----------YYAKHNNEPTDIPVpSSRSSRVGVYLDWPAGTLSFYS 1894
Cdd:cd13743     73 VGSKS----KWRLGLIKGTTSRKGKLNKSPENgvwliglkegrVYEAFANPRVPLPL-STRPQRIGVFLDYEKGELTFYN 147

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2073512899 1895 VFS-DTLTHLHTFHSTFTESLYPGFRV-WPD 1923
Cdd:cd13743    148 ADSpDELVPIYTFQAEFQGKLYPLLDVcWHE 178
SPRY_PRY_A33L cd12905
zinc-binding protein A33-like; This domain, consisting of the distinct N-terminal PRY ...
 1750-1918 3.83e-17

zinc-binding protein A33-like; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM69 and TRIM proteins NF7 and bloodthirsty (bty). TRIM69 is a novel testis E3 ubiquitin ligase that may function to ubiquitinate its particular substrates during spermatogenesis. In humans, TRIM69 localizes in the cytoplasm and nucleus, and requires an intact RING finger domain to function. TRIM protein NF7, which also contains a chromodomain (CHD) at the N-terminus and an RFP (Ret finger protein)-like domain at the C-terminus, is required for its association with transcriptional units of RNA polymerase II which is mediated by a trimeric B box. In Xenopus oocyte, xNF7 has been identified as a nuclear microtubule-associated protein (MAP) whose microtubule-bundling activity, but not E3-ligase activity, contributes to microtubule organization and spindle integrity. Bloodthirsty (bty) is a novel gene identified in zebrafish and has been shown to likely play a role in in regulation of the terminal steps of erythropoiesis.


Pssm-ID: 293962 [Multi-domain]  Cd Length: 178  Bit Score: 81.30  E-value: 3.83e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1750 PGPrkyaCELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL-SGRCYWEAeWSGDGA--EIAV 1826
Cdd:cd12905      1 PGP----APLTFDPETAHPSLILSRDLTAVTESDEMQPYPRSPKRFLQCVNVLASQGFqSGRHYWEV-WVGSKTkwDLGV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1827 AYKSIKRKEWSDesalgcndkswglFCSPHGYYA---KHNNE------P-TDIPvPSSRSSRVGVYLDWPAGTLSFYSvf 1896
Cdd:cd12905     76 ASESVDRQARVK-------------LCPENGYWTlrlRNGDEywagtqPwTRLR-VTSRPQRIGVFLDCEERKVSFYN-- 139

                          170       180
                   ....*....|....*....|..
gi 2073512899 1897 SDTLTHLHTFHSTFTESLYPGF 1918
Cdd:cd12905    140 ADDMSLLYSFHQGPRGKVFPFF 161
SPRY_PRY_TRIM72 cd13742
PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72); This domain, consisting of ...
 1758-1923 5.22e-17

PRY/SPRY domain in tripartite motif-binding protein 72 (TRIM72); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM72. Muscle-specific TRIM72 (also known as Mitsugumin 53 or MG53) has been shown to perform a critical function in membrane repair following acute muscle injury by nucleating the assembly of the repair machinery at injury sites. It is expressed specifically in skeletal muscle and heart, and tethered to the plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. TRIM72 interacts with dysferlin, a sarcolemmal protein whose deficiency causes Miyoshi myopathy (MM) and limb girdle muscular dystrophy type 2B (LGMD2B); this coordination plays an important role in the repair of sarcolemma damage.


Pssm-ID: 293976 [Multi-domain]  Cd Length: 192  Bit Score: 81.06  E-value: 5.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1758 ELTLDPNTAYRTLSLSEGNRKVTCVTKEQP-YPDHPERFDFWSQVLCREGLS-GRCYWEAEwSGDGAEIAVAYKSIKRKE 1835
Cdd:cd13742     13 NLTFDPDTAHPYLVVSSDGKRVECADQKQAvSSDDPNRFDKANCVVSHQSFSeGEHYWEVI-VGDKPRWALGVISAEAGR 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1836 WSDESALGCNDkSWGLFCSPHGYYAKH--NNEPTDIPVPsSRSSRVGVYLDWPAGTLSFY-SVFSDTLTHLHTFHSTFTE 1912
Cdd:cd13742     92 KGRLHALPSNG-FWLLGCKEGKVYEAHveHKEPRALRVE-GRPTRIGVYLSFSDGVLSFYdASDEDNLVQLFAFHERFPG 169

                          170
                   ....*....|..
gi 2073512899 1913 SLYPGFRV-WPD 1923
Cdd:cd13742    170 PLYPFFDVcWHD 181
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 1398-1729 5.53e-17

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 86.00  E-value: 5.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1398 QTLRLTDCHISDDGYVCLALTLMANPscVKELDLSNNNSG-ESAKNLLFATLKDPHLKMeeLRLAGCKLTERSYEIVASA 1476
Cdd:COG5238    156 VHLLGLAARLGLLAAISMAKALQNNS--VETVYLGCNQIGdEGIEELAEALTQNTTVTT--LWLKRNPIGDEGAEILAEA 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1477 LQSaNSPLRELDLGHSDLQQSGEMLLS-ALQSpNCKLETLRLTGCKLT---GRFLALTLQGaNPHLRELDISDGELQYSG 1552
Cdd:COG5238    232 LKG-NKSLTTLDLSNNQIGDEGVIALAeALKN-NTTVETLYLSGNQIGaegAIALAKALQG-NTTLTSLDLSVNRIGDEG 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1553 GELLHQPLNQdckvrliccrlkdsscavmasvlqfcvsqlsvldmtgcdlqtsdekllsclgnpNCQLKTLKLADCKLTE 1632
Cdd:COG5238    309 AIALAEGLQG------------------------------------------------------NKTLHTLNLAYNGIGA 334

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1633 ESCKALASTLQSSVSLTELDLTNSELKDSGIQLLSAGLSNpHCKLQTLRLSGCLITHQGCSFLASALKSNPfyLKQLDLS 1712
Cdd:COG5238    335 QGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEG-NTTLRELNLGKNNIGKQGAEALIDALQTNR--LHTLILD 411

                          330
                   ....*....|....*..
gi 2073512899 1713 YNHPGDSGVRELTDRLN 1729
Cdd:COG5238    412 GNLIGAEAQQRLEQLLE 428
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 1311-1569 9.37e-17

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 85.23  E-value: 9.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1311 QLSDLDMSGCDPQTSVEKLLS-SLGNPNCRLKILRLKGCKLTHESCKVVASFLQSANPLLELDLSNNVLRDSGVQLLSKG 1389
Cdd:COG5238    152 GGNAVHLLGLAARLGLLAAISmAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEA 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1390 LSSPHcKLQTLRLTDCHISDDGYVCLAlTLMANPSCVKELDLSNNNSGESAKNLLFATLKD-PHLKmeELRLAGCKLTER 1468
Cdd:COG5238    232 LKGNK-SLTTLDLSNNQIGDEGVIALA-EALKNNTTVETLYLSGNQIGAEGAIALAKALQGnTTLT--SLDLSVNRIGDE 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1469 SYEIVASALQSaNSPLRELDLGHSDLQQSG-EMLLSALQSpNCKLETLRLTGCKLT---GRFLALTLQGaNPHLRELDIS 1544
Cdd:COG5238    308 GAIALAEGLQG-NKTLHTLNLAYNGIGAQGaIALAKALQE-NTTLHSLDLSDNQIGdegAIALAKYLEG-NTTLRELNLG 384

                          250       260
                   ....*....|....*....|....*
gi 2073512899 1545 DGELQYSGGELLHQPLNQDCKVRLI 1569
Cdd:COG5238    385 KNNIGKQGAEALIDALQTNRLHTLI 409
SPRY_PRY_TRIM25-like cd13737
PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25)-like; This domain, ...
 1759-1930 1.57e-16

PRY/SPRY domain in tripartite motif-containing domain 25 (TRIM25)-like; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of proteins similar to TRIM25 (composed of RING/B-box/coiled-coil core and also known as RBCC proteins). TRIM25 (also called Efp) ubiquitinates the N terminus of the viral RNA receptor retinoic acid-inducible gene-I (RIG-I) in response to viral infection, leading to activation of the RIG-I signaling pathway, thus resulting in type I interferon production to limit viral replication. It has been shown that the influenza A virus targets TRIM25 and disables its antiviral function.


Pssm-ID: 293972  Cd Length: 172  Bit Score: 79.15  E-value: 1.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1759 LTLDPNTAYRTLSL-----SEGNRKVTCVTKEQPYPDhperFDFWSQVLCREGLS-GRCYWEAEWSGDGAEIAVAYKSIK 1832
Cdd:cd13737      1 LNFDPNTASEELFLfkethSVLNMGILLESFFGPCQG----FNHWPQVLCTRSLCeGCHYWEAEVSNSWVCLGVTYSYSH 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1833 RKEWSDESAL-GCNDKSWGLFCSPHGYYAKHNNepTDIPVPSSRSSRVGVYLDWPAGTLSFYSVfSDTLTHLHTFHSTFT 1911
Cdd:cd13737     77 PTGKSCIFYLiGRNPYSWCLEWDSLKFSVWHNN--IQTVVHGSYYKTIGVLLDYAAGSLTFYGV-ANTMNLIYRFLTTFT 153

                          170
                   ....*....|....*....
gi 2073512899 1912 ESLYPGFRVWPDSSVSLCQ 1930
Cdd:cd13737    154 EPLYPAVMVSSGASVTLKQ 172
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 821-881 2.19e-16

NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known.


Pssm-ID: 465501  Cd Length: 57  Bit Score: 74.91  E-value: 2.19e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2073512899  821 DVILKLAELAFKHLENGNLMFYEEDLKECGIDvsEASVYSGMCTEIFREEcvFHHKKVYCF 881
Cdd:pfam17779    1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLD--ESDLSSGLLTEILQKD--LGCEKVYSF 57
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 1531-1728 3.27e-15

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 80.22  E-value: 3.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1531 LQGANPHLRELDISDGELQYSGGELLHQPlNQDCKVRLICCRLKDSSCAVMASVLQfcvsqlsvldmtgcdlqtsdekll 1610
Cdd:COG5238    151 LGGNAVHLLGLAARLGLLAAISMAKALQN-NSVETVYLGCNQIGDEGIEELAEALT------------------------ 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1611 sclgnPNCQLKTLKLADCKLTEESCKALASTLQSSVSLTELDLTNSELKDSGIQLLSAGLSNPHcKLQTLRLSGCLITHQ 1690
Cdd:COG5238    206 -----QNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT-TVETLYLSGNQIGAE 279

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2073512899 1691 GCSFLASALKSNPfYLKQLDLSYNHPGDSGVRELTDRL 1728
Cdd:COG5238    280 GAIALAKALQGNT-TLTSLDLSVNRIGDEGAIALAEGL 316
SPRY_PRY_TRIM27 cd15814
PRY/SPRY domain in tripartite motif-containing protein 27 (TRIM27), also known as RING finger ...
 1756-1920 3.43e-15

PRY/SPRY domain in tripartite motif-containing protein 27 (TRIM27), also known as RING finger protein 76 (RNF76); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM27, also known as RING finger protein 76 (RNF76) or RET finger protein (RFP). TRIM27 domain is composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It is highly expressed in the spleen, thymus and in cells of the hematopoietic compartment. TRIM27 exhibits either nuclear or cytosolic localization depending on the cell type. TRIM27 negatively regulates nucleotide-binding oligomerization domain containing 2 (NOD2)-mediated signaling by proteasomal degradation of NOD2, suggesting that TRIM27 could be a new target for therapeutic intervention in NOD2-associated diseases such as Crohn's. High expression of TRIM27 is observed in several human cancers, including breast and endometrial cancer, where elevated TRIM27 expression predicts poor prognosis. Also, TRIM27 forms an oncogenic fusion protein with Ret proto-oncogene. It is involved in different stages of spermatogenesis and its significant expression in male germ cells and seminomas, suggests that TRIM27 may be associated with the regulation of testicular germ cell proliferation and histological-type of germ cell tumors. TRIM27 could also be a predictive marker for chemoresistance in ovarian cancer patients. In the neurotoxin model of Parkinson's disease (PD), deficiency of TRIM27 decreases apoptosis and protects dopaminergic neurons, making TRIM27 an effective potential target during the treatment of PD.


Pssm-ID: 293986 [Multi-domain]  Cd Length: 177  Bit Score: 75.50  E-value: 3.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1756 ACELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVL---CREGlsGRCYWEAEwSGDGAE--IAVAYKS 1830
Cdd:cd15814      1 SVDVTLDPDTAYPSLILSDNLRQVRYSYLQQDLPDNPERFNLFPCVLgspCFIA--GRHYWEVE-VGDKAKwtIGVCEDS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1831 IKRKEwsdesalGCNDKSWGLFCSPHGYYAKH----NNEPTDIPVPSSRsSRVGVYLDWPAGTLSFYSVFSDtlTHLHTF 1906
Cdd:cd15814     78 VCRKG-------GVTSAPQNGFWAVSLWYGKEywalTSPMTALPLRTPL-QRVGIFLDYDAGEVSFYNVTER--CHTFTF 147

                          170
                   ....*....|....*
gi 2073512899 1907 -HSTFTESLYPGFRV 1920
Cdd:cd15814    148 sHATFCGPVRPYFSL 162
SPRY_PRY_TRIM21 cd12900
PRY/SPRY domain in tripartite motif-binding protein 21 (TRIM21) also known as 52kD ...
 1755-1920 9.96e-15

PRY/SPRY domain in tripartite motif-binding protein 21 (TRIM21) also known as 52kD Ribonucleoprotein Autoantigen (Ro52); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM21, which is also known as Sjogren Syndrome Antigen A (SSA), SSA1, 52kD Ribonucleoprotein Autoantigen (Ro52, Ro/SSA, SS-A/Ro) or RING finger protein 81 (RNF81). TRIM21 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. As an E3 ligase, TRIM21 mediates target specificity in ubiquitination; it regulates type 1 interferon and proinflammatory cytokines via ubiquitination of interferon regulatory factors (IRFs). It is up-regulated at the site of autoimmune inflammation, such as cutaneous lupus lesions, indicating a central role in the tissue destructive inflammatory process. It interacts with auto-antigens in patients with Sjogren syndrome and systemic lupus erythematosus, a chronic systemic autoimmune disease characterized by the presence of autoantibodies against the protein component of the human intracellular ribonucleoprotein-RNA complexes and more specifically TRIM21, Ro60/TROVE2 and La/SSB proteins. It binds the Fc part of IgG molecules via its PRY-SPRY domain with unexpectedly high affinity.


Pssm-ID: 293957  Cd Length: 180  Bit Score: 74.15  E-value: 9.96e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1755 YACELTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGL-SGRCYWEAEWSGDGA-EIAVAYKSIK 1832
Cdd:cd12900      1 HMVHITLDPDTANPWLILSKDRRQVRLGDTHQNVPENEERFDNYPMVLGAQRFnSGKHYWEVDVTGKEAwDLGVCRDSVR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1833 RKewsDESALGCNDKSWGLFCSPHGYYA-KHNNEPTDIPVPssrSSRVGVYLDWPAGTLSFYSVfSDTLTHLHTFHS-TF 1910
Cdd:cd12900     81 RK---GQFLLSPENGFWTIWLWNKKYEAgTSPQTTLHLQVP---PCQVGIFLDYEAGVVSFYNI-TDHGSLIYTFSEcAF 153

                          170
                   ....*....|
gi 2073512899 1911 TESLYPGFRV 1920
Cdd:cd12900    154 TGPLRPFFNP 163
RING-HC_TRIM39_C-IV cd16601
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ...
 317-362 1.36e-14

RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar proteins; TRIM39, also known as RING finger protein 23 (RNF23) or testis-abundant finger protein, is an E3 ubiquitin-protein ligase that plays a role in controlling DNA damage-induced apoptosis through inhibition of the anaphase promoting complex (APC/C), a multiprotein ubiquitin ligase that controls multiple cell cycle regulators, including cyclins, geminin, and others. TRIM39 also functions as a regulator of several key processes in the proliferative cycle. It directly regulates p53 stability. It modulates cell cycle progression and DNA damage responses via stabilizing p21. Moreover, TRIM39 negatively regulates the nuclear factor kappaB (NFkappaB)-mediated signaling pathway through stabilization of Cactin, an inhibitor of NFkappaB- and Toll-like receptor (TLR)-mediated transcription, which is induced by inflammatory stimulants such as tumor necrosis factor alpha. Furthermore, TRIM39 is a MOAP-1-binding protein that can promote apoptosis signaling through stabilization of MOAP-1 via the inhibition of its poly-ubiquitination process. TRIM39 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438263 [Multi-domain]  Cd Length: 44  Bit Score: 69.44  E-value: 1.36e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2073512899  317 QSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSgpSGDYSCPQC 362
Cdd:cd16601      1 EASCSLCKEYLKDPVIIECGHNFCRACITRFWEEL--DGDFPCPQC 44
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
 320-372 1.78e-14

RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar proteins; TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5, enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into the development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. TRIM65 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438271 [Multi-domain]  Cd Length: 58  Bit Score: 69.32  E-value: 1.78e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSgPSGDYSCPQCRKRSRAQPSL 372
Cdd:cd16609      6 CSICLGLYQDPVTLPCQHSFCRACIEDHWRQK-DEGSFSCPECRAPFPEGPTL 57
SPRY_PRY_FSD1 cd12901
Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This ...
 1808-1921 2.34e-14

Fibronectin type III and SPRY containing 1 (FSD1) domain includes PRY at the N-terminus; This domain is part of the fibronectin type III and SPRY domain containing 1 (FSD1) and FSD1-like (FSD1L) proteins. These are centrosome-associated proteins that are characterized by an N-terminal coiled-coil region downstream of B-box (BBC) domain, a central fibronectin type III (FN3) domain, and C-terminal repeats in PRY/SPRY domain. The FSD1 protein associates with a subset of microtubules and may be involved in the stability and organization of microtubules during cytokinesis.


Pssm-ID: 293958  Cd Length: 207  Bit Score: 74.09  E-value: 2.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1808 SGRCYWEAEWSGDGAE--IAVAYKSIKRKEwsdesALGCNDKSWGLFCS---PHGYYAKHNNEPT--DIPVPSsrssRVG 1880
Cdd:cd12901     84 GGQHYWEVRAQKDSKAfsVGVAYRSLGKFD-----QLGKTNASWCLHVNnwlQNSFAAKHNNKAKtlDVPVPD----RIG 154

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2073512899 1881 VYLDWPAGTLSFYSVFSDTLthLHTFHSTFTESLYPGFRVW 1921
Cdd:cd12901    155 VYCDFDEGQLSFYNARTKQL--LHTFKMKFTQPVLPAFMVW 193
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 13-79 2.71e-14

PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the same fold as the pfam00531 domain. This similarity may mean that this is a protein-protein interaction domain.


Pssm-ID: 460678  Cd Length: 76  Bit Score: 69.54  E-value: 2.71e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2073512899   13 LRNTLDNLTGAEFKRFKHYLQD-----QGQIAWGKLEKADTDDTVDLMVQVYSTGAG-DIILSILKTIKHNQL 79
Cdd:pfam02758    2 LLWYLEELSEEEFKKFKSLLEDepeegLRSIPRGKLEKADRLDLADLLVEHYGEDAAvDVTIEILKKINLKDL 74
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 1405-1745 3.48e-14

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 77.14  E-value: 3.48e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1405 CHISDdgyVCLALTLMANPSCVKELDLSNNNSGESAKNLLFAT---------LKDPH-LKMEELRLAGCKLTERSYEIVA 1474
Cdd:COG5238     98 EEVSP---VALAETATAVATPPPDLRRIMAKTLEDSLILYLALprrinliqvLKDPLgGNAVHLLGLAARLGLLAAISMA 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1475 SALQsaNSPLRELDLGHSDLQQSGEMLLSALQSPNCKLETLRLTGCKLTGR---FLALTLQGaNPHLRELDISDgelqys 1551
Cdd:COG5238    175 KALQ--NNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEgaeILAEALKG-NKSLTTLDLSN------ 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1552 ggellhqplNQdckvrliccrLKDSSCAVMASVLQFCvSQLSVLDMTGCDLQTSDEKLLSCLGNPNCQLKTLKLADCKLT 1631
Cdd:COG5238    246 ---------NQ----------IGDEGVIALAEALKNN-TTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIG 305

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1632 EESCKALASTLQSSVSLTELDLTNSELKDSGIQLLSAGLSNpHCKLQTLRLSGCLITHQGCSFLASALKSNPfYLKQLDL 1711
Cdd:COG5238    306 DEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQE-NTTLHSLDLSDNQIGDEGAIALAKYLEGNT-TLRELNL 383

                          330       340       350
                   ....*....|....*....|....*....|....
gi 2073512899 1712 SYNHPGDSGVRELTDRLNDPNCKLENFRYDHGGE 1745
Cdd:COG5238    384 GKNNIGKQGAEALIDALQTNRLHTLILDGNLIGA 417
SPRY_PRY_TRIM1 cd13739
PRY/SPRY domain of tripartite motif-binding protein 1 (TRIM1) or MID2; This domain, consisting ...
 1761-1924 4.51e-14

PRY/SPRY domain of tripartite motif-binding protein 1 (TRIM1) or MID2; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM1 (also known as MID2 or midline 2). MID2 and its close homolog, TRIM18 (also known as MID1), both contain a B30.2-like domain at their C-terminus and a single fibronectin type III (FN3) motif between it and their N-terminal RBCC domain. MID2 and MID1 coiled-coil motifs mediate both homo- and heterodimerization, a prerequisite for association of the rapamycin-sensitive PP2A regulatory subunit Alpha 4 with microtubules. Mutations in MID1 have shown to cause Opitz syndrome, a disorder causing congenital anomalies such as cleft lip and palate as well as heart defects.


Pssm-ID: 293974  Cd Length: 170  Bit Score: 71.97  E-value: 4.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1761 LDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFdfwSQVLCREGL------SGRCYWE-AEWSGDGAEIAVAYKSIKR 1833
Cdd:cd13739      3 LDPKMAHKKLKISNDGLQMEKDESSLKKSHTPERF---SGTGCYGAAgnifidSGCHYWEvVVGSSTWYAIGIAYKSAPK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1834 KEWSdesalGCNDKSWGLFCSPHGYYAKHNNEPTDIPVPSsRSSRVGVYLDWPAGTLSFYSVFSDTltHLHTFHSTFTES 1913
Cdd:cd13739     80 NEWI-----GKNSSSWVFSRCNNNFVVRHNNKEMLVDVPP-QLKRLGVLLDYDNNMLSFYDPANSL--HLHTFEVSFILP 151

                          170
                   ....*....|.
gi 2073512899 1914 LYPGFRVWPDS 1924
Cdd:cd13739    152 VCPTFTIWNKS 162
RING-HC_TRIM7-like_C-IV cd16594
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and ...
 314-370 1.20e-13

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


Pssm-ID: 438256 [Multi-domain]  Cd Length: 61  Bit Score: 67.33  E-value: 1.20e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2073512899  314 TQDQSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGpsGDYSCPQCRKRSRAQP 370
Cdd:cd16594      2 LQEELTCPICLDYFTDPVTLDCGHSFCRACIARCWEEPE--TSASCPQCRETCPQRN 56
RING-HC_TRIM69_C-IV cd16611
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar ...
 313-370 2.09e-13

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


Pssm-ID: 438273 [Multi-domain]  Cd Length: 59  Bit Score: 66.32  E-value: 2.09e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2073512899  313 LTQDQSrCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSgpSGDYSCPQCRKRSRAQP 370
Cdd:cd16611      1 LTEELH-CPLCLDFFRDPVMLSCGHNFCQSCITGFWELQ--AEDTTCPECRELCQYRN 55
RING-HC_TRIM25_C-IV cd16597
RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar ...
 320-379 2.17e-13

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


Pssm-ID: 438259 [Multi-domain]  Cd Length: 71  Bit Score: 66.95  E-value: 2.17e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWsQSGPSGDYSCPQCRKRSRAQPSLNPDITMA 379
Cdd:cd16597      8 CSICLELFKDPVTLPCGHNFCGVCIEKTW-DSQHGSEYSCPQCRATFPRRPELHKNTVLR 66
SPRY_PRY_TRIM10 cd15827
PRY/SPRY domain of tripartite motif-binding protein 10 (TRIM10) also known as hematopoietic ...
 1759-1928 4.14e-13

PRY/SPRY domain of tripartite motif-binding protein 10 (TRIM10) also known as hematopoietic RING finger 1 (HERF1); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM10, also known as RING finger protein 9 (RNF9) or hematopoietic RING finger 1 (HERF1). TRIM10 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. TRIM10/HERF1 is predominantly expressed during definitive erythropoiesis and in embryonic liver, and minimally expressed in adult liver, kidney, and colon. It is critical for erythroid cell differentiation and its down-regulation leads to cell death; inhibition of TRIM10 expression blocks terminal erythroid differentiation, while its over-expression in erythroid cells induces beta-major globin expression and erythroid differentiation.


Pssm-ID: 293999 [Multi-domain]  Cd Length: 172  Bit Score: 69.47  E-value: 4.14e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1759 LTLDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREGLS-GRCYWEAEWS---GDGAEIAVAYKSIKRK 1834
Cdd:cd15827      4 ISLDPQTSHPKLLLSEDHQRARFSYKWQNSPDNPQRFDRATCVLAHDGFTgGRHTWVVSVDlahGGSCTVGVVSEDVRRK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1835 ---EWSDESALGCNDKSWGlFCSPHGYYakhnnePTDIPVpSSRSSRVGVYLDWPAGTLSFYSvfSDTLTHLHTFHSTFT 1911
Cdd:cd15827     84 gelRLRPEEGVWAVRLAWG-FVSALGSF------PTRLAL-EEQPRQVRVSLDYEVGWVTFVN--AVTQEPIYTFTASFT 153

                          170
                   ....*....|....*...
gi 2073512899 1912 ESLYPGFRVWP-DSSVSL 1928
Cdd:cd15827    154 QKVFPFFGLWGrGSSFSL 171
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 1253-1505 5.87e-13

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 73.29  E-value: 5.87e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1253 GANPHLRELDISDSELQDCGGELLHQPLNQECKVRLLCCRLKH---SSCAVVASVLQFcVSQLSDLDMS----GCDpqtS 1325
Cdd:COG5238    177 LQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPigdEGAEILAEALKG-NKSLTTLDLSnnqiGDE---G 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1326 VEKLLSSLGNpNCRLKILRLKGCKLTHESCKVVASFLQSANPLLELDLSNNVLRDSGVQLLSKGLSSPHcKLQTLRLTDC 1405
Cdd:COG5238    253 VIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYN 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1406 HISDDGYVCLALTLMANPScVKELDLSNNNSG-ESAKNLlfATLKDPHLKMEELRLAGCKLTERSYEIVASALQSANspL 1484
Cdd:COG5238    331 GIGAQGAIALAKALQENTT-LHSLDLSDNQIGdEGAIAL--AKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNR--L 405

                          250       260
                   ....*....|....*....|.
gi 2073512899 1485 RELDLGHSDLQQSGEMLLSAL 1505
Cdd:COG5238    406 HTLILDGNLIGAEAQQRLEQL 426
SPRY_PRY_TRIM4 cd15809
PRY/SPRY domain in tripartite motif-binding protein 4 (TRIM4), also known as RING finger ...
 1793-1926 8.22e-13

PRY/SPRY domain in tripartite motif-binding protein 4 (TRIM4), also known as RING finger protein 87 (RNF87); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM4 which is also known as RING finger protein 87 (RNF87). TRIM4 domain is composed of RING/B-box/coiled-coil core and also known as RBCC protein. It is a positive regulator of RIG-I-mediated interferon (IFN) induction. It regulates virus-induced IFN induction and cellular antiviral innate immunity by targeting RIG-I for K63-linked poly-ubiquitination. Over-expression of TRIM4 enhances virus-triggered activation of transcription factors IRF3 and NF-kappaB, as well as IFN-beta induction. Expression of TRIM4 differs significantly in Huntington's Disease (HD) neural cells when compared with wild-type controls, possibly impacting down-regulation of the Huntingtin (HTT) gene, which is involved in the regulation of diverse cellular activities that are impaired in Huntington's Disease (HD) cells.


Pssm-ID: 293981  Cd Length: 191  Bit Score: 69.09  E-value: 8.22e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1793 ERFDFWSQVLCREGL-SGRCYWEAEwSGDGAEIAVAYKSIKRKEWSDESALGCNDKSWGLFCSPHGYYakhnneP-TDIP 1870
Cdd:cd15809     58 ERFQHLPCVLGKNVFtSGKHYWEVE-NRDSLEIAVGVCREDVMGITDGSEMSPHVGIWAICWSSAGYR------PlTSSP 130

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1871 V-PSSRSS---RVGVYLDWPAGTLSFYSVFSDtlTHLHTFHSTFTESLYPGFRVWPDSSV 1926
Cdd:cd15809    131 VsPTKQEPalhRVGVFLDHGAGEVSFYSAVDG--VHLHTFSCPLVSRLRPFFWLSPLASL 188
RING-HC_TRIM58_C-IV cd16606
RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar ...
 316-363 1.51e-12

RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar proteins; TRIM58, also known as protein BIA2, is an erythroid E3 ubiquitin-protein ligase induced during late erythropoiesis. It binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. It may participate in the erythroblast enucleation process through regulation of nuclear polarization. TRIM58 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438268 [Multi-domain]  Cd Length: 53  Bit Score: 63.73  E-value: 1.51e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2073512899  316 DQSRCGVCEQLLRDPVITTCGHSFCRQCISSYW--SQSGPSGDYSCPQCR 363
Cdd:cd16606      1 EEARCPVCLDFLQEPVSVDCGHSFCLRCISEFCekSDSAQGGVYACPQCR 50
SPRY_PRY_TRIM76_like cd12899
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like; This domain is ...
 1761-1918 1.72e-12

PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76)-like; This domain is similar to the distinct PRY/SPRY subdomain found at the C-terminus of TRIM76, a Class I TRIM protein. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5 or myospryn or SPRYD2) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It has been suggested that TRIM76 is involved in two distinct processes, protein kinase A signaling and vesicular trafficking.


Pssm-ID: 293956 [Multi-domain]  Cd Length: 176  Bit Score: 67.50  E-value: 1.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1761 LDPNTAYRTLSLSEGNRKVTCVTKEQPYPDHPERFDFWSQVLCREG----LSGRCYWEAEwSGDGAE--IAVAYKSIKRK 1834
Cdd:cd12899      4 LNEDTAHPLLSISEDGFTVVYGEEELPARDLSFSDNSFTRCVAVMGslipVRGKHYWEVE-VDEQTEyrVGVAFEDTQRN 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1835 EWsdesaLGCNDKSWglfC-------SPHGYYAKHNNEPTDIPVpSSRSSRVGVYLDWPAGTLSFYSVfsDTLTHLHTFH 1907
Cdd:cd12899     83 GY-----LGANNTSW---CmrhiitpSRHKYEFLHNGWTPDIRI-TVPPKKIGILLDYDSGRLSFFNV--DLAQHLYTFS 151

                          170
                   ....*....|.
gi 2073512899 1908 STFTESLYPGF 1918
Cdd:cd12899    152 CQFQHFVHPCF 162
RING-HC_RNF39 cd16592
RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, ...
 315-364 2.48e-12

RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, also called protein HZFw, may play a role in prolonged long term-potentiation (LTP) maintenance. It is involved in the etiology of Behcet's disease (BD). It may also be involved in HIV-1 replication. RNF39 acts as an E3 ubiquitin ligase that inhibits retinoic acid-inducible gene-I (RIG-I)-like receptor (RLR) pathways by mediating K48-linked ubiquitination and proteasomal degradation of DDX3X (DEAD-box RNA helicase 3, X-linked). RNF39 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438254 [Multi-domain]  Cd Length: 58  Bit Score: 63.24  E-value: 2.48e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2073512899  315 QDQSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPSGD----YSCPQCRK 364
Cdd:cd16592      2 QEETTCPICLGYFKDPVILDCEHSFCRACIARHWGQEAMEGNgaegVFCPQCGE 55
SPRY_PRY_TRIM62 cd13744
PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62); This domain, consisting of ...
 1748-1918 3.13e-12

PRY/SPRY domain in tripartite motif-binding protein 62 (TRIM62); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM62. It is also called DEAR1 ductal epithelium (associated RING chromosome 1) and is involved in the morphogenesis of the mammary gland; loss of TRIM62 gene expression in breast is associated with increased risk of recurrence in early-onset breast cancer and thus, making TRIM62 a predictive biomarker. Non-small cell lung cancer lesions show a step-wise loss of TRIM62 levels during disease progression, indicating that it may play a role in the evolution of lung cancer. Decreased levels of TRIM62 also represent an independent adverse prognostic factor in AML.


Pssm-ID: 293978  Cd Length: 188  Bit Score: 67.33  E-value: 3.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1748 IKPGPrkyaCELTLDPNTAYRTLSLSEgnrKVTCVT----KEQPYPDHPERFDFWSQVLCREGLSGRC-YWE------AE 1816
Cdd:cd13744      7 IHPVP----AALTLDPVTAHQRLILSD---DCTIVAygnlHPQPLQDSPKRFDVEVSVLGSEGFSGGVhYWEvvvsekTQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1817 WSgdgaeIAVAYKSIKRKewsdeSALGCNdKSWGLFC--SPHGYYAKHNNEP-TDIPVpSSRSSRVGVYLDWPAGTLSFY 1893
Cdd:cd13744     80 WM-----IGLAHEAVSRK-----GSIQIQ-PGRGFYCivMHDGNQYSACTEPwTRLNV-KSKLEKVGVYLDYDKGLLIFY 147

                          170       180
                   ....*....|....*....|....*
gi 2073512899 1894 SvfSDTLTHLHTFHSTFTESLYPGF 1918
Cdd:cd13744    148 N--ADDMSWLYTFREKFPGKLCSYF 170
RING-HC_TRIM17_C-IV cd16595
RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar ...
 315-375 7.25e-12

RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar proteins; TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (Terf), is a crucial E3 ubiquitin ligase that is necessary and sufficient for neuronal apoptosis and contributes to Mcl-1 ubiquitination in cerebellar granule neurons (CGNs). It interacts in a SUMO-dependent manner with nuclear factor of activated T cell NFATc3 transcription factor, and thus inhibits the activity of NFATc3 by preventing its nuclear localization. In contrast, it binds to and inhibits NFATc4 transcription factor in a SUMO-independent manner. Moreover, TRIM17 stimulates degradation of kinetochore protein ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for the mitotic spindle checkpoint, and negatively regulates cell proliferation. TRIM17 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438257 [Multi-domain]  Cd Length: 70  Bit Score: 62.32  E-value: 7.25e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2073512899  315 QDQSRCGVCEQLLRDPVITTCGHSFCRQCISSYW-------SQSGPSGDYSCPQCRKRSrAQPSLNPD 375
Cdd:cd16595      3 QEEATCSICLDYFTDPVMTTCGHNFCRACIQLSWekargkkGRRKQKGSFPCPECREMS-PQRNLRPN 69
RING-HC_TRIM62_C-IV cd16608
RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar ...
 315-364 2.57e-11

RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar proteins; TRIM62, also known as Ductal Epithelium Associated Ring Chromosome 1 (DEAR1), is a cytoplasmic E3 ubiquitin-protein ligase that was identified as a dominant regulator of acinar morphogenesis in the mammary gland. It is implicated in the inflammatory response of immune cells by regulating the Toll-like receptor 4 (TLR4) signaling pathway, leading to increased activity of the activator protein 1 (AP-1) transcription factor in primary macrophages. It is also involved in muscular protein homeostasis, especially during inflammation-induced atrophy, and may play a role in the pathogenesis of ICU-acquired weakness (ICUAW) by activating and maintaining inflammation in myocytes. Moreover, TRIM62 facilitates K27-linked poly-ubiquitination of CARD9 and also regulates CARD9-mediated anti-fungal immunity and intestinal inflammation. It also functions as a chromosome 1p35 tumor suppressor and negatively regulates transforming growth factor beta (TGFbeta)-driven epithelial-mesenchymal transition (EMT) by binding to and promoting the ubiquitination of SMAD3, a major effector of TGFbeta-mediated EMT. TRIM62 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438270 [Multi-domain]  Cd Length: 52  Bit Score: 60.21  E-value: 2.57e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2073512899  315 QDQSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQsgpSGDYSCPQCRK 364
Cdd:cd16608      4 KDELLCSICLSIYQDPVSLGCEHYFCRQCITEHWSR---SEHRDCPECRR 50
RING-HC_TRIM26_C-IV cd16598
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar ...
 315-364 3.61e-11

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


Pssm-ID: 438260 [Multi-domain]  Cd Length: 64  Bit Score: 60.18  E-value: 3.61e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2073512899  315 QDQSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPSGDYSCPQCRK 364
Cdd:cd16598      2 EEEVTCSICLDYLRDPVTIDCGHNFCRSCITDYCPISGGHERPVCPLCRK 51
RING-HC_TRIM47-like_C-IV cd16604
RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar ...
 320-364 7.11e-11

RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar proteins; TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. It plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis. This subfamily also includes RING finger protein 135 (RNF135). RNF135, also known as RIG-I E3 ubiquitin ligase (REUL) or Riplet, is a widely expressed E3 ubiquitin-protein ligase that consists of an N-terminal C3HC4-type RING-HC finger and C-terminal B30.2/SPRY and PRY motifs, but lacks the B-box and coiled-coil domains that are also typically present in TRIM proteins. RNF135 serves as a specific retinoic acid-inducible gene-I (RIG-I)-interacting protein that ubiquitinates RIG-I and specifically stimulates RIG-I-mediated innate antiviral activity to produce antiviral type-I interferon (IFN) during the early phase of viral infection. It also has been identified as a bio-marker and therapy target of glioblastoma. It associates with the ERK signal transduction pathway and plays a role in glioblastoma cell proliferation, migration and cell cycle.


Pssm-ID: 438266 [Multi-domain]  Cd Length: 49  Bit Score: 58.97  E-value: 7.11e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSqSGPSGDYSCPQCRK 364
Cdd:cd16604      3 CPICLDLLKDPVTLPCGHSFCMGCLGALWG-AGRGGRASCPLCRQ 46
RING-HC_TRIM41-like_C-IV cd16602
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and ...
 315-375 9.20e-11

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


Pssm-ID: 438264 [Multi-domain]  Cd Length: 53  Bit Score: 58.78  E-value: 9.20e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2073512899  315 QDQSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSqsgpsgdYSCPQCRKrSRAQPSLNPD 375
Cdd:cd16602      1 QEEAVCAICLDYFKDPVSIGCGHNFCRVCVTQLWG-------FTCPQCRK-SFPRRSFRPN 53
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 1619-1738 1.23e-10

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 65.07  E-value: 1.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1619 QLKTLKLADCKLTEESCKALASTLQSSVSLTELDLTNSEL--KDSGIQLLSAGLSNPhCKLQTLRLSGCLITHQGCSFLA 1696
Cdd:cd00116     24 CLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETgrIPRGLQSLLQGLTKG-CGLQELDLSDNALGPDGCGVLE 102

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2073512899 1697 SALKSnpFYLKQLDLSYNHPGDSGVRELTDRLNDPNCKLENF 1738
Cdd:cd00116    103 SLLRS--SSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKL 142
SPRY_PRY_SPRYD4 cd12903
PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct ...
 1761-1921 1.28e-10

PRY/SPRY domain containing protein 4 (SPRYD4); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain and is encoded by the SPRYD4 gene. SPRYD4 (SPRY containing domain 4) is ubiquitously expressed in many human tissues, most strongly in kidney, bladder, brain, thymus and stomach. Subcellular localization demonstrates that SPRYD4 protein is localized in the nucleus when overexpressed in COS-7 green monkey cell. It has remained uncharacterized thus far.


Pssm-ID: 293960  Cd Length: 169  Bit Score: 62.08  E-value: 1.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1761 LDPNTAYRTLSLSEGNRKV---------TCVtkeqpyPDHPERFDFWSQVLCREGL-SGRCYWEAEWS-GDGAEIAVAYK 1829
Cdd:cd12903      3 LDERTAHSSLDLFKKDTGViyrmlgvdpTKV------PQNPERFRDWAVVLGDTPVtSGRHYWEVTVKrSQEFRIGVADV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1830 SIKRkewsdESALGCNDKSWGLFCSPHGYYAKHNNEPTdiPVPS-SRSSRVGVYLDWPAGTLSFysVFSDTLTHLHTFHS 1908
Cdd:cd12903     77 DMSR-----DECIGTNESSWVFAYAQRKWYAMVANETV--PVPLvGKPDRVGLLLDYEAGKLSL--VDVEKNSVVHTMSA 147

                          170
                   ....*....|...
gi 2073512899 1909 TFTESLYPGFRVW 1921
Cdd:cd12903    148 EFRGPVVPAFALW 160
RING-HC_TRIM77_C-IV cd16543
RING finger, HC subclass, found in tripartite motif-containing protein 77 (TRIM77) and similar ...
 315-370 1.84e-10

RING finger, HC subclass, found in tripartite motif-containing protein 77 (TRIM77) and similar proteins; TRIM77 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including two consecutive zinc-binding domains, a C3HC4-type RING-HC finger and Bbox2, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438205 [Multi-domain]  Cd Length: 54  Bit Score: 57.79  E-value: 1.84e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2073512899  315 QDQSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSgpSGDYSCPQCRKRSRAQP 370
Cdd:cd16543      1 EDQLTCSICLDLLKDPVTIPCGHSFCMNCITLLWDRK--QGVPSCPQCRESFPPRP 54
SPRY pfam00622
SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many ...
 1810-1918 2.45e-10

SPRY domain; SPRY Domain is named from SPla and the RYanodine Receptor and it is found in many eukaryotic proteins with a wide range of functions. It is a protein-interaction module involved in many important signalling pathways like RNA processing, regulation of histone H3 methylation, innate immunity or embryonic development. It can be divided into 11 subfamilies based on amino acid sequence similarity or the presence of additional protein domains. The greater SPRY family is divided into the SPRY/B30.2 (which contains a PRY extension at the N-terminal) and SPRY-only sub-families which are preceded by a subdomain that is structurally similar to the PRY region. SPRY/B30.2 structures revealed a bent beta-sandwich fold comprised of two beta-sheets. Distant homologs are domains in butyrophilin/ marenostrin/pyrin.


Pssm-ID: 459877  Cd Length: 121  Bit Score: 59.66  E-value: 2.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1810 RCYWEAEWSGDGAE---IAVAYKSIKRKewsDESALGCNDKSWGLfcspHGYYAK--HNNEPTDIPVPSSRS-SRVGVYL 1883
Cdd:pfam00622    1 RHYFEVEIFGQDGGgwrVGWATKSVPRK---GERFLGDESGSWGY----DGWTGKkyWASTSPLTGLPLFEPgDVIGCFL 73

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2073512899 1884 DWPAGTLSFYSVfsdTLTHLHTFHS-TFTESLYPGF 1918
Cdd:pfam00622   74 DYEAGTISFTKN---GKSLGYAFRDvPFAGPLFPAV 106
RING-HC_RNF170 cd16553
RING finger, HC subclass, found in RING finger protein 170 (RNF170) and similar proteins; ...
 317-365 1.23e-09

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


Pssm-ID: 438215 [Multi-domain]  Cd Length: 57  Bit Score: 55.76  E-value: 1.23e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2073512899  317 QSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPSGDYSCPQCRKR 365
Cdd:cd16553      1 DMECPICLQDARFPVETNCGHLFCGPCIITYWRHGSWLGAVSCPVCRQT 49
RING-HC_TRIM68_C-IV cd16610
RING finger, HC subclass, found in tripartite motif-containing protein 68 (TRIM68) and similar ...
 320-363 2.34e-09

RING finger, HC subclass, found in tripartite motif-containing protein 68 (TRIM68) and similar proteins; TRIM68, also known as RING finger protein 137 (RNF137) or SSA protein SS-56 (SS-56), is an E3 ubiquitin-protein ligase that negatively regulates Toll-like receptor (TLR)- and RIG-I-like receptor (RLR)-driven type I interferon production by degrading TRK fused gene (TFG), a novel driver of IFN-beta downstream of anti-viral detection systems. It also functions as a cofactor for androgen receptor-mediated transcription by regulating ligand-dependent transcription of androgen receptor in prostate cancer cells. Moreover, TRIM68 is a cellular target of autoantibody responses in Sjogre's syndrome (SS), as well as systemic lupus erythematosus (SLE). It is also an auto-antigen for T cells in SS and SLE. TRIM68 belongs the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438272 [Multi-domain]  Cd Length: 49  Bit Score: 54.52  E-value: 2.34e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPSGD--YSCPQCR 363
Cdd:cd16610      4 CPICMTFLREPVSIDCGHSFCHSCLSGLWEVPGESQNwgYTCPLCR 49
RING-HC_TRIM4_C-IV cd16590
RING finger, HC subclass, found in tripartite motif-containing protein TRIM4 and similar ...
 315-375 2.58e-09

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


Pssm-ID: 438252 [Multi-domain]  Cd Length: 61  Bit Score: 55.04  E-value: 2.58e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2073512899  315 QDQSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGpsGDYSCPQCRKRSrAQPSLNPD 375
Cdd:cd16590      4 QEELTCPICLDYFQDPVSIECGHNFCRGCLHRNWAPGG--GPFPCPECRHPS-APAALRPN 61
RING-HC_TRIM10_C-IV cd16593
RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar ...
 315-363 2.84e-09

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


Pssm-ID: 438255 [Multi-domain]  Cd Length: 61  Bit Score: 54.91  E-value: 2.84e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2073512899  315 QDQSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPSGDYS--CPQCR 363
Cdd:cd16593      3 ADEVNCPICQGTLREPVTIDCGHNFCRACLTRYCEIPGPDLEEPptCPLCK 53
RING-HC_TRIM38_C-IV cd16600
RING finger, HC subclass, found in tripartite motif-containing protein 38 (TRIM38) and similar ...
 320-363 3.44e-09

RING finger, HC subclass, found in tripartite motif-containing protein 38 (TRIM38) and similar proteins; TRIM38, also known as RING finger protein 15 (RNF15) or zinc finger protein RoRet, is an E3 ubiquitin-protein ligase that promotes K63- and K48-linked ubiquitination of cellular proteins and also catalyzes self-ubiquitination. It negatively regulates Tumor necrosis factor alpha (TNF-alpha)- and interleukin-1beta-triggered Nuclear factor-kappaB (NF-kappaB) activation by mediating lysosomal-dependent degradation of transforming growth factor beta (TGFbeta)-activated kinase 1 (TAK1)-binding protein (TAB)2/3, two critical components of the TAK1 kinase complex. It also inhibits TLR3/4-mediated activation of NF-kappaB and interferon regulatory factor 3 (IRF3) by mediating ubiquitin-proteasomal degradation of TNF receptor-associated factor 6 (Traf6) and NAK-associated protein 1 (Nap1), respectively. Moreover, TRIM38 negatively regulates TLR3-mediated interferon beta (IFN-beta) signaling by targeting ubiquitin-proteasomal degradation of TIR domain-containing adaptor inducing IFN-beta (TRIF). It functions as a valid target for autoantibodies in primary Sjogren's Syndrome. TRIM38 belongs the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438262 [Multi-domain]  Cd Length: 58  Bit Score: 54.39  E-value: 3.44e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYW---SQSGPSGD-YSCPQCR 363
Cdd:cd16600      8 CSICLQLMTEPVSINCGHSYCKRCIVSFLenqSQLEPGLEtFSCPQCR 55
RING-HC_TRIM40-C-V cd16583
RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar ...
 314-364 3.74e-09

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


Pssm-ID: 438245 [Multi-domain]  Cd Length: 63  Bit Score: 54.45  E-value: 3.74e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2073512899  314 TQDQSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPSGDYSCPQCRK 364
Cdd:cd16583      2 SDEEGVCPICQEPLKEAVSTDCGHLFCRMCLTQHAKKASASGVFSCPVCRK 52
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 183-469 5.54e-09

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 61.32  E-value: 5.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  183 QIGRGPSSSDKPQTHRPVSPVPSCVSMKSDWSMGRPPNFSSGPPQ-----SDPKPQTHRPVSP---VPSCVSMKSDR--- 251
Cdd:pfam03154  165 QILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQgspatSQPPNQTQSTAAPhtlIQQTPTLHPQRlps 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  252 ------SMGRPPNFSNGPPQSDPKPQTHRPVSPVPScvSMKSDRSMGRPPnfsnGPPQSDPnvwrnvLTQDQSRCgvceQ 325
Cdd:pfam03154  245 phpplqPMTQPPPPSQVSPQPLPQPSLHGQMPPMPH--SLQTGPSHMQHP----VPPQPFP------LTPQSSQS----Q 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  326 LLRDPVITTCGHSFCRQcissywsQSGPSgdYSCPQCRKRSRAQPsLNPditmaQPLlyahtttTQPHVYPPTAMAQSSL 405
Cdd:pfam03154  309 VPPGPSPAAPGQSQQRI-------HTPPS--QSQLQSQQPPREQP-LPP-----APL-------SMPHIKPPPTTPIPQL 366

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2073512899  406 yqhremaqhhlkPSTTMAQVPPHSdSGQDPlyphFHMAQISPQPPldehiVLEGSKHLQTEHAP 469
Cdd:pfam03154  367 ------------PNPQSHKHPPHL-SGPSP----FQMNSNLPPPP-----ALKPLSSLSTHHPP 408
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 1091-1410 6.19e-09

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 60.57  E-value: 6.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1091 ASALQSANSPLRELDLSHSDLQQSgemLGSALQSPNcklETLRLAGCKLTGRFLALTLQ-GANPHLRELDISDGELQDCG 1169
Cdd:COG5238    123 MAKTLEDSLILYLALPRRINLIQV---LKDPLGGNA---VHLLGLAARLGLLAAISMAKaLQNNSVETVYLGCNQIGDEG 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1170 GELLHKPLNEDCKVR---LKHSSCA-----VVASVLQFcVSQLSVLDMSGCDLQTSE-EKLPSSLGNpNCRLKTLRLAGC 1240
Cdd:COG5238    197 IEELAEALTQNTTVTtlwLKRNPIGdegaeILAEALKG-NKSLTTLDLSNNQIGDEGvIALAEALKN-NTTVETLYLSGN 274

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1241 KLT---GRFLALTLQGaNPHLRELDISDSELQDCGGELLHQPLNQECKVRLLCcrLKHSscavvasvlqfcvsQLSDldm 1317
Cdd:COG5238    275 QIGaegAIALAKALQG-NTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLN--LAYN--------------GIGA--- 334

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1318 SGCdpqtsvEKLLSSLgNPNCRLKILRLKGCKLTHESCKVVASFLQSANPLLELDLSNNVLRDSGVQLLSKGLSspHCKL 1397
Cdd:COG5238    335 QGA------IALAKAL-QENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQ--TNRL 405

                          330
                   ....*....|...
gi 2073512899 1398 QTLRLTDCHISDD 1410
Cdd:COG5238    406 HTLILDGNLIGAE 418
zf-C3HC4_4 pfam15227
zinc finger of C3HC4-type, RING; This is a family of primate-specific Ret finger protein-like ...
 320-362 7.70e-09

zinc finger of C3HC4-type, RING; This is a family of primate-specific Ret finger protein-like (RFPL) zinc-fingers of the C3HC4 type. Ret finger protein-like proteins are primate-specific target genes of Pax6, a key transcription factor for pancreas, eye and neocortex development. This domain is likely to be DNA-binding. This zinc-finger domain together with the RDM domain, pfam11002, forms a large zinc-finger structure of the RING/U-Box superfamily. RING-containing proteins are known to exert an E3 ubiquitin protein ligase activity with the zinc-finger structure being mandatory for binding to the E2 ubiquitin-conjugating enzyme.


Pssm-ID: 464570 [Multi-domain]  Cd Length: 42  Bit Score: 52.82  E-value: 7.70e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWsQSGPSGDYSCPQC 362
Cdd:pfam15227    1 CPICLDYLEKPVSIECGHSFCLSCINSLQ-KEPDGESLLCPQC 42
mRING-HC-C3HC3D_TRAF7 cd16644
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
 319-361 8.16e-09

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 7 (TRAF7) and similar proteins; TRAF7, also known as RING finger and WD repeat-containing protein 1 or RING finger protein 119 (RNF119), is an E3 ubiquitin-protein ligase involved in signal transduction pathways that lead either to activation or repression of NF-kappaB transcription factor by promoting K29-linked ubiquitination of several cellular targets, including the NF-kappaB essential modulator (NEMO) and the p65 subunit of NF-kappaB transcription factor. It is also involved in K29-linked polyubiquitination that has been implicated in lysosomal degradation of proteins. Moreover, TRAF7 is required for K48-linked ubiquitination of p53, a key tumor suppressor and a master regulator of various signaling pathways, such as those related to apoptosis, cell cycle and DNA repair. It is also required for tumor necrosis factor alpha (TNFalpha)-induced Jun N-terminal kinase activation and promotes cell death by regulating polyubiquitination and lysosomal degradation of c-FLIP protein. Furthermore, TRAF7 functions as small ubiquitin-like modifier (SUMO) E3 ligase involved in other post-translational modification, such as sumoylation. It binds to and stimulates sumoylation of the proto-oncogene product c-Myb, a transcription factor regulating proliferation and differentiation of hematopoietic cells. It potentiates MEKK3-induced AP1 and CHOP activation and induces apoptosis. Meanwhile, TRAF7 mediates MyoD1 regulation of the pathway and cell-cycle progression in myoblasts. It also plays a role in Toll-like receptors (TLR) signaling. TRAF7 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and an adjacent zinc finger, and a unique C-terminal domain that comprises a coiled coil domain and seven WD40 repeats.


Pssm-ID: 438306 [Multi-domain]  Cd Length: 47  Bit Score: 53.13  E-value: 8.16e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2073512899  319 RCGVCEQLLRDPVITTCGHSFCRQCISSywsqsgpSGDYSCPQ 361
Cdd:cd16644      7 YCPLCQRVFKDPVITSCGHTFCRRCALT-------APGEKCPV 42
RING-HC_ScPSH1-like cd16568
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated ...
 316-370 8.64e-09

RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated protein 1 (ScPSH1) and similar proteins; ScPSH1 is a Cse4-specific E3 ubiquitin ligase that interacts with the kinetochore protein Pat1 and targets the degradation of budding yeast centromeric histone H3 variant, CENP-ACse4, which is essential for faithful chromosome segregation. ScPSH1 contains a C3HC4-type RING-HC finger and a DNA directed RNA polymerase domain.


Pssm-ID: 438230 [Multi-domain]  Cd Length: 54  Bit Score: 53.14  E-value: 8.64e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2073512899  316 DQSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPSgdySCPQCRKRSRAQP 370
Cdd:cd16568      3 ETQECIICHEYLYEPMVTTCGHTYCYTCLNTWFKSNRSL---SCPDCRTKITTQP 54
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
 319-362 9.75e-09

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


Pssm-ID: 438113 [Multi-domain]  Cd Length: 41  Bit Score: 52.49  E-value: 9.75e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  319 RCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPsgdySCPQC 362
Cdd:cd16449      2 ECPICLERLKDPVLLPCGHVFCRECIRRLLESGSI----KCPIC 41
SPRY_PRY_TRIM47 cd15808
PRY/SPRY domain in tripartite motif-containing protein 47 (TRIM47), also known as RING finger ...
 1754-1909 2.32e-08

PRY/SPRY domain in tripartite motif-containing protein 47 (TRIM47), also known as RING finger protein 100 (RNF100) or Gene overexpressed in astrocytoma protein (GOA); This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM47, also known as GOA (Gene overexpressed in astrocytoma protein) or RNF100 (RING finger protein 100). TRIM47 domains are composed of RING/B-box/coiled-coil core and also known as RBCC proteins. It is highly expressed in kidney tubular cells, but lowly expressed in most tissue. It is overexpressed in astrocytoma tumor cells and plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis; astrocytoma, also known as cerebral astrocytoma, is a malignant glioma that arises from astrocytes. Genome wide studies on white matter lesions have identified a novel locus on chromosome 17q25 harboring several genes such as TRIM47 and TRIM65 which pinpoints to possible novel mechanisms leading to these lesions.


Pssm-ID: 293980  Cd Length: 206  Bit Score: 56.43  E-value: 2.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1754 KYACELTLDPNTAYRTLSL--SEGNRKVTCVTkeqPYPDHPERFDFWSQVLCREGLS-GRCYWEAEWSGDGAEIAVAYKS 1830
Cdd:cd15808      5 KFAFIVDLDSDTADKFLQLfgTKGVKRVLCPI---SYPESPTRFTHCEQVLGEGALDrGTYYWEVEIIEGWVSVGVMAED 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1831 IKRKEWSDESALGCNDKSWGLFCSPHGYYAK-HNNEPtdiPVPSSRSSRVGVYLDWPAGTLSFYSVFSDTLTHLHTFHST 1909
Cdd:cd15808     82 FSPREPYDRGRLGRNAHSCCLQWNGRNFSVWfHGLEA---PLPHPFSPTVGVCLEYADRALAFYAVRDGKVSLLRRLKAS 158
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
 320-362 2.55e-08

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: 51.36  E-value: 2.55e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 2073512899   320 CGVC-EQLLRDPVITTCGHSFCRQCISSYWSQSGPsgdySCPQC 362
Cdd:smart00184    1 CPIClEEYLKDPVILPCGHTFCRSCIRKWLESGNN----TCPIC 40
COG5222 COG5222
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
303-378 6.64e-08

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227547 [Multi-domain]  Cd Length: 427  Bit Score: 57.06  E-value: 6.64e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2073512899  303 QSDPN-VWRNVLTQDQSRCGVCEQLLRDPVIT-TCGHSFCRQCISSYWSQSgpsgDYSCPQCRKRSRAQPSLNPDITM 378
Cdd:COG5222    259 AEIPDqVYKMQPPNISLKCPLCHCLLRNPMKTpCCGHTFCDECIGTALLDS----DFKCPNCSRKDVLLDGLTPDIDK 332
RING-HC_TRIM8_C-V cd16580
RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar ...
 309-372 7.22e-08

RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar proteins; TRIM8, also known as glioblastoma-expressed RING finger protein (GERP) or RING finger protein 27 (RNF27), is a probable E3 ubiquitin-protein ligase that may promote proteasomal degradation of suppressor of cytokine signaling 1 (SOCS1) and further regulate interferon-gamma signaling. It functions as a new p53 modulator that stabilizes p53 impairing its association with MDM2 and inducing the reduction of cell proliferation. TRIM8 deficit dramatically impairs p53 stabilization and activation in response to chemotherapeutic drugs. TRIM8 also modulates tumor necrosis factor-alpha (TNFalpha) and interleukin-1beta (IL-1beta)-triggered nuclear factor-kappaB (NF- kappa B) activation by targeting transforming growth factor beta (TGFbeta) activated kinase 1 (TAK1) for K63-linked polyubiquitination. Moreover, TRIM8 modulates translocation of phosphorylated STAT3 into the nucleus through interaction with Hsp90beta and consequently regulates transcription of Nanog in embryonic stem cells. It also interacts with protein inhibitor of activated STAT3 (PIAS3), which inhibits IL-6-dependent activation of STAT3. TRIM8 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The coiled coil domain is required for homodimerization and the region immediately C-terminal to the RING motif is sufficient to mediate the interaction with SOCS1.


Pssm-ID: 438242 [Multi-domain]  Cd Length: 67  Bit Score: 51.05  E-value: 7.22e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2073512899  309 WRNVLtQDQSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSgpSGDYSCPQCRKRSRAQPSL 372
Cdd:cd16580      4 WKNCF-EEELICPICLHVFVEPVQLPCKHNFCRGCIGEAWAKD--AGLVRCPECNQAYNQKPSL 64
RING-HC_RAD16-like cd16567
RING finger, HC subclass, found in Saccharomyces cerevisiae DNA repair protein RAD16, ...
 320-364 7.42e-08

RING finger, HC subclass, found in Saccharomyces cerevisiae DNA repair protein RAD16, Schizosaccharomyces pombe rhp16, and similar proteins; Budding yeast RAD16, also known as ATP-dependent helicase RAD16, is encoded by a yeast excision repair gene homologous to the recombinational repair gene RAD54 and to the SNF2 gene involved in transcriptional activation. It is a component of the global genome repair (GGR) complex that promotes global genome nucleotide excision repair (GG-NER) by removing DNA damage from non-transcribing DNA. RAD16 is involved in differential repair of DNA after UV damage, and repairs preferentially the MAT-alpha locus compared with the HML-alpha locus. Fission yeast rhp16, also known as ATP-dependent helicase rhp16, is a RAD16 homolog. It is involved in GGR via nucleotide excision repair (NER), in conjunction with rhp7, after UV irradiation. Both RAD16 and rhp16 contain a C3HC4-type RING-HC finger, as well as a DEAD-like helicase domain and a helicase superfamily C-terminal domain.


Pssm-ID: 438229 [Multi-domain]  Cd Length: 48  Bit Score: 50.42  E-value: 7.42e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYwSQSGPSGDYSCPQCRK 364
Cdd:cd16567      3 CGICHEEAEDPVVARCHHVFCRACVKEY-IESAPGGKVTCPTCHK 46
RING-HC_TRIM35_C-IV cd16599
RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar ...
 319-366 1.29e-07

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


Pssm-ID: 438261 [Multi-domain]  Cd Length: 66  Bit Score: 50.15  E-value: 1.29e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2073512899  319 RCGVCEQLLRDPVITTCGHSFCRQCISSYWSQsgpSGDYSCPQCRKRS 366
Cdd:cd16599      6 LCPICYEPFREAVTLRCGHNFCKGCVSRSWER---QPRAPCPVCKEAS 50
SPRY_PRY_TRIM76 cd12898
PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called ...
 1809-1918 1.37e-07

PRY/SPRY domain in tripartite motif-containing protein 76 (TRIM76), also called cardiomyopathy-associated protein 5; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM76, a Class I TRIM protein. TRIM76 (also known as cardiomyopathy-associated protein 5 or CMYA5 or myospryn or SPRYD2) is a muscle-specific member of the TRIM superfamily, but lacks the RING domain. It has been suggested that TRIM76 is involved in two distinct processes, protein kinase A signaling and vesicular trafficking. It has also been implicated in Duchenne muscular dystrophy and cardiac disease; gene polymorphism of TRIM76 is associated with left ventricular wall thickness in patients with hypertension while its interactions with M-band titin and calpain 3 link it to tibial and limb-girdle muscular dystrophies.


Pssm-ID: 293955  Cd Length: 171  Bit Score: 53.39  E-value: 1.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1809 GRCYWEAEWS-GDGAEIAVAYKSIKRKewsdeSALGCNDKSWGLFCSPHG----YYAKHNNEPTDIPVpSSRSSRVGVYL 1883
Cdd:cd12898     52 GQYYWETTVTrCPAYRLGICSSSASQA-----GALGEGSTSWCLHCVPTSepcrYTLLHSGIVSDVFV-TERPARVGTLL 125

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2073512899 1884 DWPAGTLSFYSVFSDTLthLHTFHSTFTESLYPGF 1918
Cdd:cd12898    126 DYNNGRLIFINAESGQL--LGIFRHRFAQPCHPAF 158
RING-HC_TRIM5-like_C-IV cd16591
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, ...
 315-365 1.53e-07

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


Pssm-ID: 438253 [Multi-domain]  Cd Length: 72  Bit Score: 50.13  E-value: 1.53e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2073512899  315 QDQSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQS-GPSGDYSCPQCRKR 365
Cdd:cd16591      4 KEEVTCPICLELLTEPLSLDCGHSFCQACITANHKESvNQEGESSCPVCRTS 55
RING-HC_BAR cd16497
RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as ...
 320-371 1.63e-07

RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as RING finger protein 47, was originally identified as an inhibitor of Bax-induced apoptosis. It participates in the block of apoptosis induced by TNF-family death receptors (extrinsic pathway) and mitochondria-dependent apoptosis (intrinsic pathway). BAR is predominantly expressed by neurons in the central nervous system and is involved in the regulation of neuronal survival. It is an endoplasmic reticulum (ER)-associated RING-type E3 ubiquitin ligase that interacts with BI-1 protein and post-translationally regulates its stability, as well as functioning in ER stress. BAR contains an N-terminal C3HC4-type RING-HC finger, a SAM domain, a coiled-coil domain, and a C-terminal transmembrane (TM) domain. This model corresponds to the RING-HC finger responsible for the binding of ubiquitin conjugating enzymes (E2s).


Pssm-ID: 438160 [Multi-domain]  Cd Length: 52  Bit Score: 49.43  E-value: 1.63e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPSgdySCPQCRKRSRAQPS 371
Cdd:cd16497      4 CHCCYDLLVNPTTLNCGHSFCRHCLALWWKSSKKT---ECPECRQKWEGFPK 52
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
 320-364 2.58e-07

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


Pssm-ID: 438161 [Multi-domain]  Cd Length: 94  Bit Score: 50.37  E-value: 2.58e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSgpSGDYSCPQCRK 364
Cdd:cd16498     19 CPICLELLKEPVSTKCDHQFCRFCILKLLQKK--KKPAPCPLCKK 61
RING-HC_TRIM21_C-IV cd16596
RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar ...
 320-364 2.87e-07

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


Pssm-ID: 438258 [Multi-domain]  Cd Length: 77  Bit Score: 49.51  E-value: 2.87e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCIssywSQSGPSGDYSCPQCRK 364
Cdd:cd16596     12 CPICLDPFVEPVSIECGHSFCQECI----SQVGKGGGSVCPVCRQ 52
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1361-1765 2.95e-07

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 54.94  E-value: 2.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1361 FLQSANPLLELDLSNNVLRDSGVQLLSKGLSSPHCKLQTLRLTDCHISDDGYVCLALTLMANPSCVKELDLSNNNSGESA 1440
Cdd:COG4886     33 LLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNL 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1441 KNLlfatlkdphlkmEELRLAGCKLTERSYEIvaSALQSanspLRELDLGHSDLQQSGEMLlsalqsPNCK-LETLRLTG 1519
Cdd:COG4886    113 TNL------------ESLDLSGNQLTDLPEEL--ANLTN----LKELDLSNNQLTDLPEPL------GNLTnLKSLDLSN 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1520 CKLTGrfLALTLqGANPHLRELDISDGELQYsggelLHQPLNQdckvrliccrLKdsscavmasvlqfcvsQLSVLDMTG 1599
Cdd:COG4886    169 NQLTD--LPEEL-GNLTNLKELDLSNNQITD-----LPEPLGN----------LT----------------NLEELDLSG 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1600 CDLQTSDEKLLSClgnpnCQLKTLKLADCKLTEesckalASTLQSSVSLTELDLTNSELKDsgiqlLSAGLSNPhcKLQT 1679
Cdd:COG4886    215 NQLTDLPEPLANL-----TNLETLDLSNNQLTD------LPELGNLTNLEELDLSNNQLTD-----LPPLANLT--NLKT 276

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1680 LRLSGCLITHQGCSFLASALKSNPFYLKQLDLSYNHPGDSGVRELTDRLNDPNCKLENFRYDHGGEFRIKPGPRKYACEL 1759
Cdd:COG4886    277 LDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLL 356


                   ....*.
gi 2073512899 1760 TLDPNT 1765
Cdd:COG4886    357 NLLSLL 362
RING-HC_RNF125 cd16542
RING finger, HC subclass, found in RING finger protein 125 (RNF125); RNF125, also known as ...
 320-369 3.25e-07

RING finger, HC subclass, found in RING finger protein 125 (RNF125); RNF125, also known as T-cell RING activation protein 1 (TRAC-1), is an E3 ubiquitin-protein ligase that is predominantly expressed in lymphoid cells, and functions as a positive regulator of T cell activation. It also down-modulates HIV replication and inhibits pathogen-induced cytokine production. It negatively regulates type I interferon signaling, which conjugates Lys(48)-linked ubiquitination to retinoic acid-inducible gene-I (RIG-I) and subsequently leads to the proteasome-dependent degradation of RIG-I. Further, RNF125 conjugates ubiquitin to melanoma differentiation-associated gene 5 (MDA5), a family protein of RIG-I. It thus acts as a negative regulator of RIG-I signaling, and is a direct target of miR-15b in the context of Japanese encephalitis virus (JEV) infection. Moreover, RNF125 binds to and ubiquitinates JAK1, prompting its degradation and inhibition of receptor tyrosine kinase (RTK) expression. It also negatively regulates p53 function through physical interaction and ubiquitin-mediated proteasome degradation. Mutations in RNF125 may lead to overgrowth syndromes (OGS). RNF125, together with three closely related proteins: RNF114, RNF138 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM). The UIM of RNF125 binds K48-linked poly-ubiquitin chains and is, together with the RING domain, required for auto-ubiquitination.


Pssm-ID: 438204 [Multi-domain]  Cd Length: 50  Bit Score: 48.72  E-value: 3.25e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSywsqSGPSGDYSCPQCRKRSRAQ 369
Cdd:cd16542      4 CAVCLEVLHQPVRTRCGHVFCRPCIAT----SLRNNTWTCPYCRAYLSSE 49
RING-HC_LONFs_rpt1 cd16513
first RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
 319-368 4.28e-07

first RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger protein family; The LON peptidase N-terminal domain and RING finger protein family includes LONRF1 (also known as RING finger protein 191 or RNF191), LONRF2 (also known as RING finger protein 192, RNF192, or neuroblastoma apoptosis-related protease), LONRF3 (also known as RING finger protein 127 or RNF127), which are characterized by containing two C3HC4-type RING-HC fingers, four tetratricopeptide (TPR) repeats, and an ATP-dependent protease La (LON) substrate-binding domain at the C-terminus. Their biological functions remain unclear. This model corresponds to the first RING-HC finger.


Pssm-ID: 438176 [Multi-domain]  Cd Length: 47  Bit Score: 48.07  E-value: 4.28e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2073512899  319 RCGVCEQLLRDPVITTCGHSFCRQCISsywsqsgPSGDYSCPQCRKRSRA 368
Cdd:cd16513      4 SCPLCRGLLFEPVTLPCGHTFCKRCLE-------RDPSSRCRLCRLKLSP 46
RING-HC_CHR27-like cd23142
RING finger, HC subclass, found in Arabidopsis thaliana protein CHROMATIN REMODELING 27 (CHR27) ...
 319-365 5.36e-07

RING finger, HC subclass, found in Arabidopsis thaliana protein CHROMATIN REMODELING 27 (CHR27) and similar proteins; CHR27, also called protein SNF2-RING-HELICASE-LIKE 1, is a probable helicase-like transcription factor involved in transcriptional gene silencing. It associates with SUVR2 and contributes to transcriptional gene silencing at RNA-directed DNA methylation (RdDM) target loci but also at RdDM-independent target loci. It may be involved in nucleosome positioning to form ordered nucleosome arrays on chromatin. It associates with SUVR2 and functions redundantly with FRG2. It is required for the efficient methylation of a broad range of RdDM target loci. CHR27 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438504 [Multi-domain]  Cd Length: 55  Bit Score: 48.34  E-value: 5.36e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2073512899  319 RCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPSGDY-SCPQCRKR 365
Cdd:cd23142      2 ICPICNDPPEDAVVTLCGHVFCCECVFQYLSSDRTCRQFnHCPLCRQK 49
RING-HC_TRIM60-like_C-IV cd16607
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM60, TRIM61, TRIM75 ...
 317-363 7.02e-07

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM60, TRIM61, TRIM75 and similar proteins; TRIM60, also known as RING finger protein 129 (RNF129) or RING finger protein 33 (RNF33), is a cytoplasmic protein expressed in the testis. It may play an important role in the spermatogenesis process, the development of the preimplantation embryo, and in testicular functions. RNF33 interacts with the cytoplasmic kinesin motor proteins KIF3A and KIF3B suggesting possible contribution to cargo movement along the microtubule in the expressed sites. It is also involved in spermatogenesis in Sertoli cells under the regulation of nuclear factor-kappaB (NF-kappaB). TRIM75 mainly localizes within spindles, suggesting it may function in spindle organization and thereby affect meiosis. Both TRIM60 and TRIM75 belong the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B2-box, and two coiled coil domains, as well as a PRY domain and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast, TRIM61 belongs to the C-V subclass of the TRIM family that contains RBCC domains only. Its biological function remains unclear.


Pssm-ID: 438269 [Multi-domain]  Cd Length: 48  Bit Score: 47.80  E-value: 7.02e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2073512899  317 QSRCGVCEQLLRDPVITTCGHSFCRQCISSYWsqSGPSGDYSCPQCR 363
Cdd:cd16607      1 EASCPICLDYLKDPVTINCGHNFCRSCISMSW--KDLQDTFPCPVCR 45
RING-HC_TRIM43-like_C-IV cd16603
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM43, TRIM48, TRIM49, ...
 315-375 7.05e-07

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


Pssm-ID: 438265 [Multi-domain]  Cd Length: 59  Bit Score: 47.86  E-value: 7.05e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2073512899  315 QDQSRCGVCEQLLRDPVITTCGHSFCRQCISSYWsQSGPSgDYSCPQCRKRSRaQPSLNPD 375
Cdd:cd16603      2 QRELTCPICMNYFIDPVTIDCGHSFCRPCLYLNW-QDIPF-LAQCPECRKTTE-QRNLKTN 59
SPRY_PRY_TRIM67_9 cd12889
PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, ...
 1760-1893 9.65e-07

PRY/SPRY domain in tripartite motif-containing proteins, TRIM9 and TRIM67; This domain, consisting of the distinct N-terminal PRY subdomain followed by the SPRY subdomain, is found at the C-terminus of TRIM9 proteins. TRIM9 protein is expressed mainly in the cerebral cortex, and functions as an E3 ubiquitin ligase. It has been shown that TRIM9 is localized to the neurons in the normal human brain and its immunoreactivity in affected brain areas in Parkinson's disease and dementia with Lewy bodies is severely decreased, possibly playing an important role in the regulation of neuronal function and participating in pathological process of Lewy body disease through its ligase. TRIM67 negatively regulates Ras activity via degradation of 80K-H, leading to neural differentiation, including neuritogenesis.


Pssm-ID: 293947  Cd Length: 172  Bit Score: 50.70  E-value: 9.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1760 TLDPNTAYRTLSLSEGNRKVTCVTKEQpypdhperfdfwSQVLCREGLS-GRCYWEA-----EWSGDGAeIAVAYKSIKR 1833
Cdd:cd12889     11 TFDPSTSHPDIILSNDNMTVTCNSYED------------RVVLGSVGFSrGVHYWEVtidryDGHPDPA-FGVARIDVNK 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2073512899 1834 kewsdESALGCNDKSWGLFCSPHGYYAKHNNEPTD-IPVPSSRSSRVGVYLDWPAGTLSFY 1893
Cdd:cd12889     78 -----DKMLGKDDKGWSMYIDNNRSWFLHNNEHSNrTEGGITVGSVVGVLLDLDRHTLSFY 133
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
 316-363 9.86e-07

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 53.47  E-value: 9.86e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2073512899  316 DQS-RCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGpsgdySCPQCR 363
Cdd:TIGR00599   24 DTSlRCHICKDFFDVPVLTSCSHTFCSLCIRRCLSNQP-----KCPLCR 67
RING-HC_COP1 cd16504
RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and ...
 320-362 1.17e-06

RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and similar proteins; COP1, also known as RING finger and WD repeat domain protein 2 (RFWD2) or RING finger protein 200 (RNF200), is a central regulator of photomorphogenic development in plants, which targets key transcription factors for proteasome-dependent degradation. It is localized predominantly in the nucleus, but may also be present in the cytosol. Mammalian COP1 functions as an E3 ubiquitin-protein ligase that interacts with Jun transcription factors and modulates their transcriptional activity. It also interacts with and negatively regulates the tumor-suppressor protein p53. Moreover, COP1 associates with COP9 signalosome subunit 6 (CSN6), and is involved in 14-3-3sigma ubiquitin-mediated degradation. The CSN6-COP1 link enhances ubiquitin-mediated degradation of p27(Kip1), a critical CDK inhibitor involved in cell cycle regulation, to promote cancer cell growth. Furthermore, COP1 functions as the negative regulator of ETV1 and influences prognosis in triple-negative breast cancer. COP1 contains an N-terminal extension, a C3HC4-type RING-HC finger, a coiled coil domain, and seven WD40 repeats. In human COP1, a classic leucine-rich NES, and a novel bipartite NLS is bridged by the RING-HC finger.


Pssm-ID: 438167 [Multi-domain]  Cd Length: 47  Bit Score: 46.85  E-value: 1.17e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGpsgdySCPQC 362
Cdd:cd16504      5 CPICFDIIKEAFVTKCGHSFCYKCIVKHLEQKN-----RCPKC 42
PHA03247 PHA03247
large tegument protein UL36; Provisional
 182-451 1.41e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.79  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  182 SQIGRGPSSSDKPQTHRPVSPVPSCVSMKSdwsMGRPPnfssgPPQSDPKPQTHRPVSPVPSCVSMKSDRSMGRPPNFSN 261
Cdd:PHA03247  2668 RRLGRAAQASSPPQRPRRRAARPTVGSLTS---LADPP-----PPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAP 2739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  262 GPPqsdPKPQThrPVSPVpscvsmkSDRSMGRPPNFSnGPPQSDPnvwrnvltqdqSRCGVCEQLLRDPVITTCGHSFCR 341
Cdd:PHA03247  2740 APP---AVPAG--PATPG-------GPARPARPPTTA-GPPAPAP-----------PAAPAAGPPRRLTRPAVASLSESR 2795

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  342 QCISSYWSQSGPSGDYSCPQCRKRSRAQPS-LNPDITMAQPLL-------YAHTTTTQPHVYP-------------PTAM 400
Cdd:PHA03247  2796 ESLPSPWDPADPPAAVLAPAAALPPAASPAgPLPPPTSAQPTApppppgpPPPSLPLGGSVAPggdvrrrppsrspAAKP 2875

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2073512899  401 AQSSLYQHREMAQHHLKPSTTMAQVPPHS-------DSGQDPLYPHFHMAQISPQPPL 451
Cdd:PHA03247  2876 AAPARPPVRRLARPAVSRSTESFALPPDQperppqpQAPPPPQPQPQPPPPPQPQPPP 2933
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
 320-360 1.60e-06

RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.


Pssm-ID: 463881 [Multi-domain]  Cd Length: 38  Bit Score: 46.24  E-value: 1.60e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2073512899  320 CGVCEQLLRDPViTTCGHSFCRQCIssYWSQSGPSGDYSCP 360
Cdd:pfam13445    1 CPICLELFTDPV-LPCGHTFCRECL--EEMSQKKGGKFKCP 38
RING-HC_AtRMA-like cd16745
RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) ...
 320-363 1.99e-06

RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) and similar proteins; AtRMAs, including AtRma1, AtRma2, and AtRma3, are endoplasmic reticulum (ER)-localized Arabidopsis homologs of human outer membrane of the ER-anchor E3 ubiquitin-protein ligase, RING finger protein 5 (RNF5). AtRMAs possess E3 ubiquitin ligase activity, and may play a role in the growth and development of Arabidopsis. The AtRMA1 and AtRMA3 genes are predominantly expressed in major tissues, such as cotyledons, leaves, shoot-root junction, roots, and anthers, while AtRMA2 expression is restricted to the root tips and leaf hydathodes. AtRma1 probably functions with the Ubc4/5 subfamily of E2. AtRma2 is likely involved in the cellular regulation of ABP1 expression levels through interacting with auxin binding protein 1 (ABP1). AtRMA proteins contain an N-terminal C3HC4-type RING-HC finger and a trans-membrane-anchoring domain in their extreme C-terminal region.


Pssm-ID: 438403 [Multi-domain]  Cd Length: 45  Bit Score: 46.32  E-value: 1.99e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSyWSQSGPSgDYSCPQCR 363
Cdd:cd16745      3 CNICLDLAQDPVVTLCGHLFCWPCLHK-WLRRQSS-QPECPVCK 44
RING-HC_RAG1 cd16530
RING finger, HC subclass, found in recombination activating gene-1 (RAG-1) and similar ...
 320-363 2.29e-06

RING finger, HC subclass, found in recombination activating gene-1 (RAG-1) and similar proteins; RAG-1, also known as V(D)J recombination-activating protein 1, RING finger protein 74 (RNF74), or endonuclease RAG1, is the catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. RAG1 is a lymphoid-specific factor that mediates DNA-binding to conserved recombination signal sequences (RSS) and catalyzes DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. It also functions as an E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H3, which is required for the joining step of V(D)J recombination. RAG-1 contains an N-terminal C3HC4-type RING-HC finger that mediates monoubiquitylation of histone H3, an adjacent C2H2-type zinc finger, and a nonamer binding (NBD) DNA-binding domain.


Pssm-ID: 319444 [Multi-domain]  Cd Length: 46  Bit Score: 46.28  E-value: 2.29e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPsgdySCPQCR 363
Cdd:cd16530      5 CQVCEHILADPVQTPCKHLFCRTCILKCLKVMGS----YCPSCR 44
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1101-1484 2.67e-06

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 51.86  E-value: 2.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1101 LRELDLSHSDLQQSGEMLGSaLQspncKLETLRLAGCKLTGRFLALtlqGANPHLRELDISDGELQDCGGELLhkplned 1180
Cdd:COG4886    115 LESLDLSGNQLTDLPEELAN-LT----NLKELDLSNNQLTDLPEPL---GNLTNLKSLDLSNNQLTDLPEELG------- 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1181 ckvRLKhsscavvasvlqfcvsQLSVLDMSGCDLQTseekLPSSLGNPNcRLKTLRLAGCKLTGrfLALTLqGANPHLRE 1260
Cdd:COG4886    180 ---NLT----------------NLKELDLSNNQITD----LPEPLGNLT-NLEELDLSGNQLTD--LPEPL-ANLTNLET 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1261 LDISDSELQDcggellhqplnqeckvrllccrlkhsscavVASVLQFcvSQLSDLDMSGcdpqTSVEKLLSSLGNPNcrL 1340
Cdd:COG4886    233 LDLSNNQLTD------------------------------LPELGNL--TNLEELDLSN----NQLTDLPPLANLTN--L 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1341 KILRLKGCKLTHESCKVVASFLQSANPLLELDLSNNVLrdsgVQLLSKGLSSPHCKLQTLRLTDCHISDDGYVCLALTLM 1420
Cdd:COG4886    275 KTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLE----LLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALL 350

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2073512899 1421 ANPSCVKELDLSNNNSGESAKNLLFATLKDPHLKMEELRLAGCKLTERSYEIVASALQSANSPL 1484
Cdd:COG4886    351 TLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAVNTE 414
RING-HC_HLTF cd16509
RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar ...
 315-363 3.12e-06

RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar proteins; HLTF, also known as DNA-binding protein/plasminogen activator inhibitor 1 regulator, HIP116, RING finger protein 80, SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3, or sucrose nonfermenting protein 2-like 3, is a yeast RAD5 homolog found in mammals. It has both E3 ubiquitin ligase and DNA helicase activities, and plays a pivotal role in the template-switching pathway of DNA damage tolerance. It is involved in Lys-63-linked poly-ubiquitination of proliferating cell nuclear antigen (PCNA) at Lys-164 and in the regulation of DNA damage tolerance. It shows double-stranded DNA translocase activity with 3'-5' polarity, thereby facilitating regression of the replication fork. HLTF contains an N-terminal HIRAN (HIP116 and RAD5 N-terminal) domain, a SWI/SNF helicase domain that is divided into N- and C-terminal parts by an insertion of a C3HC4-type RING-HC finger involved in the poly-ubiquitination of PCNA.


Pssm-ID: 438172 [Multi-domain]  Cd Length: 53  Bit Score: 45.76  E-value: 3.12e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2073512899  315 QDQSRCGVCEQLLRDPVITTCGHSFCRQCIssywSQSGPSGDYSCPQCR 363
Cdd:cd16509      1 GSDEECAICLDSLTNPVITPCAHVFCRRCI----CEVIQREKAKCPMCR 45
RING-HC_TRIM72_C-IV cd16612
RING finger, HC subclass, found in tripartite motif-containing protein 72 (TRIM72) and similar ...
 315-369 3.24e-06

RING finger, HC subclass, found in tripartite motif-containing protein 72 (TRIM72) and similar proteins; TRIM72, also known as Mitsugumin-53 (MG53), is a muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at muscle injury sites. It is required in repair of alveolar epithelial cells under plasma membrane stress failure. It interacts with dysferlin to regulate sarcolemmal repair. Upregulation of TRIM72 develops obesity, systemic insulin resistance, dyslipidemia, and hyperglycemia, as well as induces diabetic cardiomyopathy through transcriptional activation of the peroxisome proliferation-activated receptor alpha (PPAR-alpha) signaling pathway. Compensation for the absence of AKT signaling by ERK signaling during TRIM72 overexpression leads to pathological hypertrophy. Moreover, TRIM72 functions as a novel negative feedback regulator of myogenesis by targeting insulin receptor substrate-1 (IRS-1). It is transcriptionally activated by the synergism of myogenin (MyoD) and myocyte enhancer factor 2 (MEF2). TRIM72 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438274 [Multi-domain]  Cd Length: 60  Bit Score: 46.27  E-value: 3.24e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2073512899  315 QDQSrCGVCEQLLRDPVITTCGHSFCRQCISSYwSQSGPSGDYSCPQCRKRSRAQ 369
Cdd:cd16612      3 QDLS-CPLCLKLFQSPVTTECGHTFCQDCLSRV-PKEEDGGSTSCPTCQAPTKPE 55
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1109-1531 3.68e-06

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 51.47  E-value: 3.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1109 SDLQQSGEMLGSALQSPNCKLETLRLAGCKLTGRFlaltlqganPHLRELDISDGELQDCGGELlhkplnedckVRLKHs 1188
Cdd:COG4886     78 SLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNL---------TNLESLDLSGNQLTDLPEEL----------ANLTN- 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1189 scavvasvlqfcvsqLSVLDMSGCDLQTseekLPSSLGN-PNcrLKTLRLAGCKLTGrfLALTLqGANPHLRELDISDSE 1267
Cdd:COG4886    138 ---------------LKELDLSNNQLTD----LPEPLGNlTN--LKSLDLSNNQLTD--LPEEL-GNLTNLKELDLSNNQ 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1268 LQDcggelLHQPLNQeckvrllCCRLKhsscavvasVLQFCVSQLSDLDMSgcdpqtsveklLSSLGNpncrLKILRLKG 1347
Cdd:COG4886    194 ITD-----LPEPLGN-------LTNLE---------ELDLSGNQLTDLPEP-----------LANLTN----LETLDLSN 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1348 CKLTHesckvVASFLQSANpLLELDLSNNVLRDsgvqlLSKGLSSPhcKLQTLRLTDCHISDdgyvcLALTLMANPSCVK 1427
Cdd:COG4886    238 NQLTD-----LPELGNLTN-LEELDLSNNQLTD-----LPPLANLT--NLKTLDLSNNQLTD-----LKLKELELLLGLN 299

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1428 ELDLSNNNSGESAKNLLFATLKDPHLKMEELRLAGCKLTERSYEIVASALQSANSPLRELDLGHSDLQQSGEMLLSALQS 1507
Cdd:COG4886    300 SLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATL 379

                          410       420
                   ....*....|....*....|....
gi 2073512899 1508 PNCKLETLRLTGCKLTGRFLALTL 1531
Cdd:COG4886    380 LTLALLLLTLLLLLLTTTAGVLLL 403
PHA03247 PHA03247
large tegument protein UL36; Provisional
 185-460 9.90e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 9.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  185 GRGPSSSDKPQTHRPVSPVPScvsmksdwsmGRPPNFSSGPPQSDPKPQTHRPV-SPVPSCVSM-KSDRSMGRPPNFSnG 262
Cdd:PHA03247  2610 GPAPPSPLPPDTHAPDPPPPS----------PSPAANEPDPHPPPTVPPPERPRdDPAPGRVSRpRRARRLGRAAQAS-S 2678

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  263 PPQSdPKPQTHRP-VSPVPscvsmksdrSMGRPPNfSNGPPQSDPNVWRNVL---TQDQSRCGVCEQLLRDPVITTcghs 338
Cdd:PHA03247  2679 PPQR-PRRRAARPtVGSLT---------SLADPPP-PPPTPEPAPHALVSATplpPGPAAARQASPALPAAPAPPA---- 2743

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  339 fcrqcissywSQSGPSGDYScpQCRKRSRAQPSLNPDITM-AQPLLYAHTTTTQPHVyPPTAMAQSSLYQHREMAQHHLK 417
Cdd:PHA03247  2744 ----------VPAGPATPGG--PARPARPPTTAGPPAPAPpAAPAAGPPRRLTRPAV-ASLSESRESLPSPWDPADPPAA 2810

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2073512899  418 PSTTMAQVPPhSDSGQDPLYPHFHMAQISPQP---PLDEHIVLEGS 460
Cdd:PHA03247  2811 VLAPAAALPP-AASPAGPLPPPTSAQPTAPPPppgPPPPSLPLGGS 2855
RING-HC_RNF113A_B cd16539
RING finger, HC subclass, found in RING finger proteins RNF113A, RNF113B, and similar proteins; ...
 320-364 1.12e-05

RING finger, HC subclass, found in RING finger proteins RNF113A, RNF113B, and similar proteins; RNF113A, also known as zinc finger protein 183 (ZNF183), is an E3 ubiquitin-protein ligase that physically interacts with the E2 protein, UBE2U. A nonsense mutation in RNF113A is associated with an X-linked trichothiodystrophy (TTD). Its yeast ortholog Cwc24p is predicted to have a spliceosome function and acts in a complex with Cef1p to participate in pre-U3 snoRNA splicing, indirectly affecting pre-rRNA processing. It is also important for the U2 snRNP binding to primary transcripts and co-migrates with spliceosomes. Moreover, the ortholog of RNF113A in fruit flies may also act as a spliceosome and is hypothesized to be involved in splicing, namely within the central nervous system. The ortholog in Caenorhabditis elegans is involved in DNA repair of inter-strand crosslinks. RNF113B, also known as zinc finger protein 183-like 1, shows high sequence similarity with RNF113A. Both RNF113A and RNF113B contain a CCCH-type zinc finger, which is commonly found in RNA-binding proteins involved in splicing, and a C3HC4-type RING-HC finger, which is frequently found in E3 ubiquitin ligases.


Pssm-ID: 438201 [Multi-domain]  Cd Length: 54  Bit Score: 44.50  E-value: 1.12e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGpsgdySCPQCRK 364
Cdd:cd16539      8 CFICRKPFKNPVVTKCGHYFCEKCALKHYRKSK-----KCFVCGK 47
COG5152 COG5152
Uncharacterized conserved protein, contains RING and CCCH-type Zn-fingers [General function ...
 320-376 1.13e-05

Uncharacterized conserved protein, contains RING and CCCH-type Zn-fingers [General function prediction only];


Pssm-ID: 227481 [Multi-domain]  Cd Length: 259  Bit Score: 48.92  E-value: 1.13e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQC-ISSYwsQSGPsgdySCPQCRKRSRAQPSLNPDI 376
Cdd:COG5152    199 CGICKKDYESPVVTECGHSFCSLCaIRKY--QKGD----ECGVCGKATYGRFWVVSDL 250
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
 320-362 1.18e-05

Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid. Many proteins containing a RING finger play a key role in the ubiquitination pathway.


Pssm-ID: 395049 [Multi-domain]  Cd Length: 40  Bit Score: 43.88  E-value: 1.18e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  320 CGVCEQLLRDPV-ITTCGHSFCRQCISSYWSqsgpSGDYSCPQC 362
Cdd:pfam00097    1 CPICLEEPKDPVtLLPCGHLFCSKCIRSWLE----SGNVTCPLC 40
RING-HC_LONFs_rpt2 cd16514
second RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
 320-363 1.23e-05

second RING finger, HC subclass, found in the LON peptidase N-terminal domain and RING finger protein family; The LON peptidase N-terminal domain and RING finger protein family includes LONRF1 (also known as RING finger protein 191 or RNF191), LONRF2 (also known as RING finger protein 192, RNF192, or neuroblastoma apoptosis-related protease), LONRF3 (also known as RING finger protein 127 or RNF127), which are characterized by containing two C3HC4-type RING-HC fingers, four tetratricopeptide (TPR) repeats, and an ATP-dependent protease La (LON) substrate-binding domain at the C-terminus. Their biological functions remain unclear. This model corresponds to the second RING-HC finger.


Pssm-ID: 438177 [Multi-domain]  Cd Length: 45  Bit Score: 44.18  E-value: 1.23e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPsgdysCPQCR 363
Cdd:cd16514      4 CSLCLRLLYEPVTTPCGHTFCRACLERCLDHSPK-----CPLCR 42
RING-HC_TRIM13_like_C-V cd16581
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and ...
 320-363 1.32e-05

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and similar proteins; TRIM13 and TRIM59, two closely related tripartite motif-containing proteins, belong to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, followed by a C-terminal transmembrane domain. TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts with proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis.


Pssm-ID: 438243 [Multi-domain]  Cd Length: 50  Bit Score: 44.04  E-value: 1.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPS--GDYSCPQCR 363
Cdd:cd16581      5 CSICYNIFDDPKILPCSHTFCKNCLEKLLAASGYYllASLKCPTCR 50
RING-HC_TRIM9 cd16755
RING finger, HC subclass, found in tripartite motif-containing protein 9 (TRIM9) and similar ...
 315-364 1.33e-05

RING finger, HC subclass, found in tripartite motif-containing protein 9 (TRIM9) and similar proteins; TRIM9, human ortholog of rat Spring, also known as RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in the neurodegenerative disorders through its ligase activity. It interacts with the WD repeat region of beta-transducin repeat-containing protein (beta-TrCP) through its N-terminal degron motif depending on the phosphorylation status, and thus negatively regulates nuclear factor-kappaB (NF-kappaB) activation in the NF-kappaB pro-inflammatory signaling pathway. Moreover, TRIM9 acts as a critical catalytic link between Netrin-1 and the exocytic soluble NSF attachment receptor protein (SNARE) machinery in murine cortical neurons. It promotes SNARE-mediated vesicle fusion and axon branching in a Netrin-dependent manner. TRIM9 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438413 [Multi-domain]  Cd Length: 55  Bit Score: 44.25  E-value: 1.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2073512899  315 QDQSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQS----GPSGDYSCPQCRK 364
Cdd:cd16755      1 EEELKCPVCGSFYREPIILPCSHNLCLACARNILVQTpeaeSPQSCLTCPQCHR 54
RING-HC_CHFR cd16503
RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein ...
 320-364 1.36e-05

RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also known as RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22, and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression, and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated (FHA) domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438166 [Multi-domain]  Cd Length: 55  Bit Score: 44.28  E-value: 1.36e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2073512899  320 CGVCEQLLRDPVITT-CGHSFCRQCISSYWSQSgpsgDYSCPQCRK 364
Cdd:cd16503      5 CSICQDLLHDCVSLQpCMHNFCAACYSDWMERS----NTECPTCRA 46
mRING-HC-C3HC3D_TRAF6 cd16643
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
 320-360 1.39e-05

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 6 (TRAF6) and similar proteins; TRAF6, also known as interleukin-1 signal transducer or RING finger protein 85 (RNF85), is a cytoplasmic adapter protein that mediates signals induced by the tumor necrosis factor receptor (TNFR) superfamily and Toll-like receptor (TLR)/interleukin-1 receptor (IL-1R) family. It functions as a mediator involved in the activation of mitogen-activated protein kinase (MAPK), phosphoinositide 3-kinase (PI3K), and interferon regulatory factor pathways, as well as in IL-1R-mediated activation of NF-kappaB. TRAF6 is also an oncogene that plays a vital role in K-RAS-mediated oncogenesis. TRAF6 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain.


Pssm-ID: 438305 [Multi-domain]  Cd Length: 58  Bit Score: 44.29  E-value: 1.39e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPsgdySCP 360
Cdd:cd16643      4 CPICLMALREPVQTPCGHRFCKACILKSIREAGH----KCP 40
RING-HC_ScRAD18-like cd23148
RING finger, HC subclass, found in Saccharomyces cerevisiae radiation sensitivity protein 18 ...
 319-363 1.48e-05

RING finger, HC subclass, found in Saccharomyces cerevisiae radiation sensitivity protein 18 (RAD18) and similar proteins; RAD18, also called RING-type E3 ubiquitin transferase RAD18, acts as a postreplication repair E3 ubiquitin-protein ligase that associates with the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA. The UBC2-RAD18 complex cooperates with RAD5 and the UBC13-MMS2 dimer to attach mono-ubiquitin chains on 'Lys-164' of POL30, which is necessary for PRR. The UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine. RAD18 is an E3 RING-finger protein belonging to the UBC2/RAD6 epistasis group. It contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438510 [Multi-domain]  Cd Length: 52  Bit Score: 44.06  E-value: 1.48e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2073512899  319 RCGVCEQLLRDPVITTCGHSFCRQCISSYWSQsgpsgDYSCPQCR 363
Cdd:cd23148      5 RCHICKDLLKAPMRTPCNHTFCSFCIRTHLNN-----DARCPLCK 44
RING-HC_LNX3 cd16718
RING finger, HC subclass, found in ligand of numb protein X 3 (LNX3); LNX3, also known as PDZ ...
 319-364 1.48e-05

RING finger, HC subclass, found in ligand of numb protein X 3 (LNX3); LNX3, also known as PDZ domain-containing RING finger protein 3 (PDZRN3), or Semaphorin cytoplasmic domain-associated protein 3 (SEMACAP3), is an E3 ubiquitin-protein ligase that was first identified as a Semaphorin-binding partner. It is also responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX3 acts as a negative regulator of osteoblast differentiation by inhibiting Wnt-beta-catenin signaling. LNX3 also plays an important role in neuromuscular junction formation. It interacts with and ubiquitinates the muscle specific tyrosine kinase (MuSK), thus promoting its endocytosis and negatively regulating the cell surface expression of this key regulator of postsynaptic assembly. LNX3 contains an N-terminal C3HC4-type RING-HC finger, two PDZ domains, and a C-terminal LNX3 homology (LNX3H) domain.


Pssm-ID: 438378 [Multi-domain]  Cd Length: 47  Bit Score: 43.82  E-value: 1.48e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2073512899  319 RCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGpsgdySCP-QCRK 364
Cdd:cd16718      6 KCNLCNKVLEDPLTTPCGHVFCAGCVLPWVVQQG-----SCPvKCQR 47
RING-HC_RING1-like cd16531
RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and ...
 319-375 1.50e-05

RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and similar proteins; RING1, also known as polycomb complex protein RING1, RING finger protein 1 (RNF1), or RING finger protein 1A (RING1A), is a transcriptional repressor that is associated with the Polycomb group (PcG) protein complex involved in stable repression of gene activity. RING2, also known as huntingtin-interacting protein 2-interacting protein 3, HIP2-interacting protein 3, protein DinG, RING finger protein 1B (RING1B), RING finger protein 2 (RNF2), or RING finger protein BAP-1, is an E3 ubiquitin-protein ligase that interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve the specific monoubiquitination of K119 on histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation. Both RING1 and RING2 are core components of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. RING2 acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. Members of this family contain a C3HC4-type RING-HC finger.


Pssm-ID: 438193 [Multi-domain]  Cd Length: 66  Bit Score: 44.57  E-value: 1.50e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2073512899  319 RCGVCEQLLRDP-VITTCGHSFCRQCISSYWSqsgpSGDYSCPQCRKRSRAQPSLNPD 375
Cdd:cd16531      3 MCPICLGIIKNTmTVKECLHRFCAECIEKALR----LGNKECPTCRKHLPSRRSLRPD 56
RING-HC_ORTHRUS_rpt1 cd23138
first RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; ...
 316-363 1.57e-05

first RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; This subfamily includes Arabidopsis thaliana ORTHRUS 1-5. They are E3 ubiquitin-protein ligases that may participate in CpG methylation-dependent transcriptional regulation and/or epigenetic transcriptional silencing. ORTHRUS 1 mediates ubiquitination with the E2 ubiquitin-conjugating enzymes UBC11, UBC8 and UBC8 homologs (e.g. UBC10, UBC11, UBC28 and UBC29) but not with UBC27, UBC30, UBC32, UBC34 and UBC36. ORTHRUS 2 and 5 mediate ubiquitination with the E2 ubiquitin-conjugating enzyme UBC11. ORTHRUS 1 and 2 promote methylation-mediated gene silencing leading, for example, to early flowering. They can bind to CpG, CpNpG, and CpNpN DNA motifs, with a strong preference for methylated forms, and with highest affinity for CpG substrates. Members of this subfamily contain two typical C3HC4-type RING-HC fingers. This model corresponds to the first one.


Pssm-ID: 438500 [Multi-domain]  Cd Length: 48  Bit Score: 43.97  E-value: 1.57e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2073512899  316 DQSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQsgpsGDYSCPQCR 363
Cdd:cd23138      1 DELNCSFCMQLPERPVTTPCGHNFCLKCFQKWMGQ----GKKTCGTCR 44
RING-HC_RNF5-like cd16534
RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 ...
 320-363 2.44e-05

RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 and RNF185 are E3 ubiquitin-protein ligases that are anchored to the outer membrane of the endoplasmic reticulum (ER). RNF5 acts at early stages of cystic fibrosis (CF) transmembrane conductance regulator (CFTR) biosynthesis, and functions as a target for therapeutic modalities to antagonize mutant CFTR proteins in CF patients carrying the F508del allele. RNF185 controls the degradation of CFTR and CFTR F508del allele in a RING- and proteasome-dependent manner, but does not control that of other classical endoplasmic reticulum-associated degradation (ERAD) model substrates. Moreover, both RNF5 and RNF185 play important roles in cell adhesion and migration through the modulation of cell migration by ubiquitinating paxillin. Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) are also included in this family. They possess E3 ubiquitin-protein ligase activity and may play a role in the growth and development of Arabidopsis. All members of this family contain a C3HC4-type RING-HC finger.


Pssm-ID: 438196 [Multi-domain]  Cd Length: 44  Bit Score: 43.06  E-value: 2.44e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSyWSQSGPSGDYsCPQCR 363
Cdd:cd16534      3 CNICLDTASDPVVTMCGHLFCWPCLYQ-WLETRPDRQT-CPVCK 44
RING-HC_RNF138 cd16544
RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; ...
 320-365 3.57e-05

RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; RNF138, also known as Nemo-like kinase-associated RING finger protein (NARF) or NLK-associated RING finger protein, is an E3 ubiquitin-protein ligase that plays an important role in glioma cell proliferation, apoptosis, and cell cycle. It specifically cooperates with the E2 conjugating enzyme E2-25K (Hip-2/UbcH1), regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF), and further suppresses Wnt-beta-catenin signaling. RNF138, together with three closely related proteins: RNF114, RNF125 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 438206 [Multi-domain]  Cd Length: 53  Bit Score: 42.78  E-value: 3.57e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2073512899  320 CGVCEQLLRDPV-ITTCGHSFCRQCISSYWSQSGpsgdYSCPQCRKR 365
Cdd:cd16544      5 CPVCQEVLKDPVeLPPCRHIFCKACILLALRSSG----ARCPLCRGP 47
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
319-363 4.17e-05

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 48.16  E-value: 4.17e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2073512899  319 RCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGpsgdySCPQCR 363
Cdd:COG5432     27 RCRICDCRISIPCETTCGHTFCSLCIRRHLGTQP-----FCPVCR 66
RING-HC_RNFT1 cd16741
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 ...
 320-363 4.97e-05

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 (RNFT1); RNFT1, also known as protein PTD016, is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear.


Pssm-ID: 438399 [Multi-domain]  Cd Length: 58  Bit Score: 42.57  E-value: 4.97e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQsgpsgDYSCPQCR 363
Cdd:cd16741     17 CAICQAEFRKPILLICQHVFCEECISLWFNR-----EKTCPLCR 55
RING-HC_LNX3-like cd16512
RING finger, HC subclass, found in ligand of Numb protein LNX3, LNX4, and similar proteins; ...
 319-364 5.09e-05

RING finger, HC subclass, found in ligand of Numb protein LNX3, LNX4, and similar proteins; The ligand of Numb protein X (LNX) family, also known as PDZ and RING (PDZRN) family, includes LNX1-5, which can interact with Numb, a key regulator of neurogenesis and neuronal differentiation. LNX5 (also known as PDZK4, or PDZRN4L) shows high sequence homology to LNX3 and LNX4, but it lacks the RING domain. LNX1-4 proteins function as E3 ubiquitin ligases and have a unique domain architecture consisting of an N-terminal RING-HC finger for E3 ubiquitin ligase activity and either two or four PDZ domains necessary for the substrate-binding. This family corresponds to LNX3/LNX4-like proteins, which contains a C3HC4-type RING-HC finger and two PDZ domains.


Pssm-ID: 438175 [Multi-domain]  Cd Length: 43  Bit Score: 42.40  E-value: 5.09e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2073512899  319 RCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGpsgdySCP-QCRK 364
Cdd:cd16512      2 KCKLCLGVLEEPLATPCGHVFCAGCVLPWVVRNG-----SCPlKCEP 43
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
319-362 5.62e-05

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 404756 [Multi-domain]  Cd Length: 40  Bit Score: 42.04  E-value: 5.62e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2073512899  319 RCGVCEQLLRDPVITT-CGHSFCRQCISSYWSQSGpsgdySCPQC 362
Cdd:pfam13923    1 MCPICMDMLKDPSTTTpCGHVFCQDCILRALRAGN-----ECPLC 40
vRING-HC-C4C4_RBBP6 cd16620
Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) ...
 316-364 5.84e-05

Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) and similar proteins; RBBP6, also known as proliferation potential-related protein, protein P2P-R, retinoblastoma-binding Q protein 1 (RBQ-1), or p53-associated cellular protein of testis (PACT), is a nuclear E3 ubiquitin-protein ligase involved in multiple processes, such as the control of gene expression, mitosis, cell differentiation, and cell apoptosis. It plays a role in both promoting and inhibiting apoptosis in many human cancers, including esophageal, lung, hepatocellular, and colon cancers, familial myeloproliferative neoplasms, as well as in human immunodeficiency virus-associated nephropathy (HIVAN). It functions as an Rb- and p53-binding protein that plays an important role in chaperone-mediated ubiquitination and possibly in protein quality control. It acts as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in an increase of MDM2-mediated ubiquitination and degradation of p53/TP53, and leading to both apoptosis and cell growth. It is also a double-stranded RNA-binding protein that plays a role in mRNA processing by regulating the human polyadenylation machinery and modulating expression of mRNAs with AU-rich 3' untranslated regions (UTRs). Moreover, RBBP6 ubiquitinates and destabilizes the transcriptional repressor ZBTB38 that negatively regulates transcription and levels of the MCM10 replication factor on chromatin. Furthermore, RBBP6 is involved in tunicamycin-induced apoptosis by mediating protein kinase (PKR) activation. RBBP6 contains an N-terminal ubiquitin-like domain and a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger. RBBP6 interacts with chaperones Hsp70 and Hsp40 through its N-terminal ubiquitin-like domain. It promotes the ubiquitination of p53 by Hdm2 in an E4-like manner through its RING finger. It also interacts directly with the pro-proliferative transcription factor Y-box-binding protein-1 (YB-1) via its RING finger.


Pssm-ID: 438282 [Multi-domain]  Cd Length: 55  Bit Score: 42.39  E-value: 5.84e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2073512899  316 DQSRCGVCEQLLRDPVITT-CGHSFCRQCISSYWSQSgpsgDYSCPQCRK 364
Cdd:cd16620      2 DELKCPICKDLMKDAVLTPcCGNSFCDECIRTALLEE----DFTCPTCKE 47
RING-HC_TRIM31_C-V cd16582
RING finger, HC subclass, found in tripartite motif-containing protein 31 (TRIM31) and similar ...
 320-362 6.56e-05

RING finger, HC subclass, found in tripartite motif-containing protein 31 (TRIM31) and similar proteins; TRIM31 is an E3 ubiquitin-protein ligase that primarily localizes to the cytoplasm, but is also associated with the mitochondria. It can negatively regulate cell proliferation and may be a potential biomarker of gastric cancer as it is overexpressed from the early stage of gastric carcinogenesis. TRIM31 is downregulated in non-small cell lung cancer and serves as a potential tumor suppressor. It interacts with p52 (Shc) and inhibits Src-induced anchorage-independent growth. TRIM31 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 438244 [Multi-domain]  Cd Length: 44  Bit Score: 42.12  E-value: 6.56e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSgpSGDYSCPQC 362
Cdd:cd16582      4 CPICLDILQKPVTIDCGHNFCLQCITQIGETS--CGFFKCPLC 44
RING-HC_RNF112 cd16538
RING finger, HC subclass, found in RING finger protein 112 (RNF112) and similar proteins; ...
 320-364 7.18e-05

RING finger, HC subclass, found in RING finger protein 112 (RNF112) and similar proteins; RNF112, also known as brain finger protein (BFP), zinc finger protein 179 (ZNF179), or neurolastin, is a peripheral membrane protein that is predominantly expressed in the central nervous system and localizes to endosomes. It contains functional GTPase and C3HC4-type RING-HC finger domains and has been identified as a brain-specific dynamin family GTPase that affects endosome size and spine density. Moreover, RNF112 acts as a downstream target of sigma-1 receptor (Sig-1R) regulation and may play a novel role in neuroprotection by mediating the neuroprotective effects of dehydroepiandrosterone (DHEA) and its sulfated analog (DHEAS).


Pssm-ID: 438200 [Multi-domain]  Cd Length: 52  Bit Score: 42.29  E-value: 7.18e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYwsQSGPSGDYSCPQCRK 364
Cdd:cd16538      5 CSICLERLREPISLDCGHDFCIRCFSTH--RIPGCEPPCCPECRK 47
RING-HC_RNF222 cd16564
RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; ...
 318-364 7.33e-05

RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; RNF222 is an uncharacterized C3HC4-type RING-HC finger-containing protein. It may function as an E3 ubiquitin-protein ligase.


Pssm-ID: 438226 [Multi-domain]  Cd Length: 50  Bit Score: 42.00  E-value: 7.33e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2073512899  318 SRCGVC-EQLLRDPVITTCGHSFCRQCISSYWSQSgpsgDYSCPQCRK 364
Cdd:cd16564      1 SECPVCyEDFDDAPRILSCGHSFCEDCLVKQLVSM----TISCPICRR 44
RING-HC_RNF213 cd16561
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ...
 320-363 7.47e-05

RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; RNF213, also known as ALK lymphoma oligomerization partner on chromosome 17 or Moyamoya steno-occlusive disease-associated AAA+ and RING finger protein (mysterin), is an intracellular soluble protein that functions as an E3 ubiquitin-protein ligase and AAA+ ATPase, which possibly contributes to vascular development through mechanical processes in the cell. It plays a unique role in endothelial cells for proper gene expression in response to inflammatory signals from the environment. Mutations in RNF213 may be associated with Moyamoya disease (MMD), an idiopathic cerebrovascular occlusive disorder prevalent in East Asia. It also acts as a nuclear marker for acanthomorph phylogeny. RNF213 contains two tandem enzymatically active AAA+ ATPase modules and a C3HC4-type RING-HC finger. It can form a huge ring-shaped oligomeric complex.


Pssm-ID: 438223 [Multi-domain]  Cd Length: 50  Bit Score: 41.88  E-value: 7.47e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSyWSQsgpsGDYSCPQCR 363
Cdd:cd16561      5 CSICLEDLNDPVKLPCDHVFCEECIRQ-WLP----GQMSCPLCR 43
RING-HC_PCGF cd16525
RING finger, HC subclass, found in Polycomb Group RING finger homologs (PCGF1, 2, 3, 4, 5 and ...
 320-363 8.55e-05

RING finger, HC subclass, found in Polycomb Group RING finger homologs (PCGF1, 2, 3, 4, 5 and 6), and similar proteins; This subfamily includes six Polycomb Group (PcG) RING finger homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) that use epigenetic mechanisms to maintain or repress expression of their target genes. They were first discovered in fruit flies and are well known for silencing Hox genes through modulation of chromatin structure during embryonic development. PCGF homologs play important roles in cell proliferation, differentiation, and tumorigenesis. They all have been found to associate with ring finger protein 2 (RNF2). The RNF2-PCGF heterodimer is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF homologs are critical components in the assembly of distinct Polycomb Repression Complex 1 (PRC1) related complexes which is involved in the maintenance of gene repression and which target different genes through distinct mechanisms. The Drosophila PRC1 core complex is formed by the Polycomb (Pc), Polyhomeotic (Ph), Posterior sex combs (Psc), and Sex combs extra (Sce, also known as Ring) subunits. In mammals, the composition of PRC1 is much more diverse and varies depending on the cellular context. All PRC1 complexes contain homologs of the Drosophila Ring protein. Ring1A/RNF1 and Ring1B/RNF2 are E3 ubiquitin ligases that mark lysine 119 of histone H2A with a single ubiquitin group (H2AK119ub). Mammalian homologs of the Drosophila Psc protein, such as PCGF2/Mel-18 or PCGF4/BMI1, regulate PRC1 enzymatic activity. PRC1 complexes can be divided into at least two classes according to the presence or absence of CBX proteins, which are homologs of Drosophila Pc. Canonical PRC1 complexes contain CBX proteins that recognize and bind H3K27me3, the mark deposited by PRC2. Therefore, canonical PRC1 complexes and PRC2 can act together to repress gene transcription and maintain this repression through cell division. Non-canonical PRC1 complexes, containing RYBP (together with additional proteins, such as L3mbtl2 or Kdm2b) rather than the CBX proteins have recently been described in mammals. PCGF homologs contain a C3HC4-type RING-HC finger.


Pssm-ID: 438188 [Multi-domain]  Cd Length: 42  Bit Score: 41.44  E-value: 8.55e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2073512899  320 CGVCEQLLRDPV-ITTCGHSFCRQCISSYWSQSgpsgdYSCPQCR 363
Cdd:cd16525      3 CSLCKGYLIDATtITECLHSFCKSCIVRHLETS-----KNCPVCD 42
RING-HC_TRIM9-like_C-I cd16576
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM9, TRIM67, and ...
 315-364 1.08e-04

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM9, TRIM67, and similar proteins; Tripartite motif-containing proteins TRIM9 and TRIM67 belong to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, consisting of three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM9 (the human ortholog of rat Spring), also known as RING finger protein 91 (RNF91), is a brain-specific E3 ubiquitin-protein ligase collaborating with an E2 ubiquitin conjugating enzyme UBCH5b. TRIM9 plays an important role in the regulation of neuronal functions and participates in neurodegenerative disorders through its ligase activity. TRIM67, also known as TRIM9-like protein (TNL), is a protein selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H, also known as glucosidase II beta, a protein kinase C substrate.


Pssm-ID: 438238 [Multi-domain]  Cd Length: 42  Bit Score: 41.24  E-value: 1.08e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2073512899  315 QDQSRCGVCEQLLRDPVITTCGHSFCRQCISSYwsqsgpsgDYSCPQCRK 364
Cdd:cd16576      1 EEELKCPVCGSLFTEPVILPCSHNLCLGCALNI--------QLTCPICHK 42
RING-HC_TRIM67 cd16758
RING finger, HC subclass, found in tripartite motif-containing protein 67 (TRIM67) and similar ...
 315-364 1.13e-04

RING finger, HC subclass, found in tripartite motif-containing protein 67 (TRIM67) and similar proteins; TRIM67, also known as TRIM9-like protein (TNL), is selectively expressed in the cerebellum. It interacts with PRG-1, an important molecule in the control of hippocampal excitability dependent on presynaptic LPA2 receptor signaling, and 80K-H (also known as glucosidase II beta), a protein kinase C substrate. It negatively regulates Ras signaling in cell proliferation via degradation of 80K-H, leading to neural differentiation including neuritogenesis. TRIM67 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438416 [Multi-domain]  Cd Length: 57  Bit Score: 41.61  E-value: 1.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2073512899  315 QDQSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQS-------GPSGDYSCPQCRK 364
Cdd:cd16758      1 EEELKCPVCGSLFREPIILPCSHNVCLPCARTIAVQTpeseqhlPHSSSITCPQCHR 57
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 1081-1184 1.22e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 46.71  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1081 KLSERSFEIVASALQSaNSPLRELDLSHSDLQQSG-EMLGSALQSpNCKLETLRLAGCKLTG---RFLALTLQgANPHLR 1156
Cdd:COG5238    275 QIGAEGAIALAKALQG-NTTLTSLDLSVNRIGDEGaIALAEGLQG-NKTLHTLNLAYNGIGAqgaIALAKALQ-ENTTLH 351

                           90       100
                   ....*....|....*....|....*...
gi 2073512899 1157 ELDISDGELQDCGGELLHKPLNEDCKVR 1184
Cdd:COG5238    352 SLDLSDNQIGDEGAIALAKYLEGNTTLR 379
zf-RING_5 pfam14634
zinc-RING finger domain;
319-364 1.24e-04

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 41.26  E-value: 1.24e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2073512899  319 RCGVCEQLL---RDPVITTCGHSFCRQCISSYwsqsgpSGDYSCPQCRK 364
Cdd:pfam14634    1 HCNKCFKELsktRPFYLTSCGHIFCEECLTRL------LQERQCPICKK 43
RING-HC_Bre1-like cd16499
RING finger, HC subclass, found in yeast Bre1 and its homologs from eukaryotes; Bre1 is an E3 ...
 319-344 1.26e-04

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


Pssm-ID: 438162 [Multi-domain]  Cd Length: 59  Bit Score: 41.39  E-value: 1.26e-04
                           10        20
                   ....*....|....*....|....*.
gi 2073512899  319 RCGVCEQLLRDPVITTCGHSFCRQCI 344
Cdd:cd16499      8 KCSVCNDRFKDVIITKCGHVFCNECV 33
RING-HC_UHRF cd16613
RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing ...
 320-363 1.28e-04

RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing proteins, UHRF1 and UHRF2, and similar proteins; UHRF1 is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma (LSCC), gastric cancer (GC), esophageal squamous cell carcinoma (ESCC), colorectal cancer, prostate cancer, and breast cancer. UHRF1 acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumor suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of transcription factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF2 was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation, but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) by interacting with the HBV core protein and promoting its degradation. Both UHRF1 and UHRF2 contain an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET- and RING-associated (SRA) domain, and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438275 [Multi-domain]  Cd Length: 46  Bit Score: 41.18  E-value: 1.28e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCIssywSQSGPSGDYSCPQCR 363
Cdd:cd16613      3 CICCQELVYKPITTPCKHNICKSCL----QRSFKAEVYTCPACR 42
mRING-HC-C3HC3D_LNX1-like cd16637
Modified RING finger, HC subclass (C3HC3D-type), found in ligand of Numb protein LNX1, LNX2, ...
 320-347 1.30e-04

Modified RING finger, HC subclass (C3HC3D-type), found in ligand of Numb protein LNX1, LNX2, and similar proteins; The ligand of Numb protein X (LNX) family, also known as PDZ and RING (PDZRN) family, includes LNX1-5, which can interact with Numb, a key regulator of neurogenesis and neuronal differentiation. LNX5 (also known as PDZK4 or PDZRN4L) shows high sequence homology to LNX3 and LNX4, but it lacks the RING domain. LNX1-4 proteins function as E3 ubiquitin ligases and have a unique domain architecture consisting of an N-terminal RING-HC finger for E3 ubiquitin ligase activity and either two or four PDZ domains necessary for substrate-binding. LNX1/LNX2-like proteins contain a modified C3HC3D-type RING-HC finger and four PDZ domains. This model corresponds to the RING finger.


Pssm-ID: 438299 [Multi-domain]  Cd Length: 42  Bit Score: 40.84  E-value: 1.30e-04
                           10        20
                   ....*....|....*....|....*...
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSY 347
Cdd:cd16637      4 CHICLQPLVEPLDTPCGHTFCYKCLTNY 31
RING-HC_PEX10 cd16527
RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known ...
 318-369 1.38e-04

RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known as peroxisome biogenesis factor 10, peroxisomal biogenesis factor 10, peroxisome assembly protein 10, or RING finger protein 69 (RNF69), is an integral peroxisomal membrane protein with two transmembrane regions and a C3HC4-type RING-HC finger within its cytoplasmically exposed C-terminus. It plays an essential role in peroxisome assembly, import of target substrates, and recycling or degradation of protein complexes and amino acids. It is an essential component of the spinal locomotor circuit, and thus its mutations may be involved in peroxisomal biogenesis disorders (PBD). Mutations in human PEX10 also result in autosomal recessive ataxia. Moreover, PEX10 functions as an E3-ubiquitin ligase with an E2, UBCH5C. It mono- or poly-ubiquitinates PEX5, a key player in peroxisomal matrix protein import, in a UBC4-dependent manner, to control PEX5 receptor recycling or degradation. It also links the E2 ubiquitin conjugating enzyme PEX4 to the protein import machinery of the peroxisome.


Pssm-ID: 438190 [Multi-domain]  Cd Length: 52  Bit Score: 41.06  E-value: 1.38e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2073512899  318 SRCGVCEQLLRDPVITTCGHSFCRQCISSyWSQSGPsgdySCPQCRKRSRAQ 369
Cdd:cd16527      1 RKCSLCLEERRHPTATPCGHLFCWSCITE-WCNEKP----ECPLCREPFQPQ 47
RING-HC_RNFT1-like cd16532
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein ...
 318-363 1.43e-04

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein RNFT1, RNFT2, and similar proteins; Both RNFT1 and RNFT2 are multi-pass membrane proteins containing a C3HC4-type RING-HC finger. Their biological roles remain unclear.


Pssm-ID: 438194 [Multi-domain]  Cd Length: 41  Bit Score: 40.75  E-value: 1.43e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2073512899  318 SRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQsgpsgDYSCPQCR 363
Cdd:cd16532      1 DICPICQDEFKDPVVLRCKHIFCEDCVSEWFER-----ERTCPLCR 41
PHA03247 PHA03247
large tegument protein UL36; Provisional
 188-306 1.48e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 1.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  188 PSSSDKPQTHRPVSPVPSCVSMKSDWSMG-----RPPnfsSGPPQSDPKPQTHRPVSPVPSCVSMKSDRSMGRPPNFSNG 262
Cdd:PHA03247  2831 PTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvrrRPP---SRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPER 2907

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  263 PPQSDPKPQTHRPVSPVPSCVSMKSDRSMGRPPnfSNGPPQSDP 306
Cdd:PHA03247  2908 PPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQ--PPLAPTTDP 2949
RING-HC_RNF5 cd16743
RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins; RNF5, ...
 320-363 2.48e-04

RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins; RNF5, also known as protein G16 or Ram1, is an E3 ubiquitin-protein ligase anchored to the outer membrane of the endoplasmic reticulum (ER). It acts at early stages of cystic fibrosis (CF) transmembrane conductance regulator (CFTR) biosynthesis and functions as a target for therapeutic modalities to antagonize mutant CFTR proteins in CF patients carrying the F508del allele. It also regulates the turnover of specific G protein-coupled receptors by ubiquitinating JNK-associated membrane protein (JAMP) and preventing proteasome recruitment. RNF5 limits basal levels of autophagy and influences susceptibility to bacterial infection through the regulation of ATG4B stability. It is also involved in the degradation of Pendrin, a transmembrane chloride/anion exchanger highly expressed in thyroid, kidney, and inner ear. RNF5 plays an important role in cell adhesion and migration. It can modulate cell migration by ubiquitinating paxillin. Furthermore, RNF5 interacts with virus-induced signaling adaptor (VISA) at mitochondria in a viral infection-dependent manner, and further targets VISA at K362 and K461 for K48-linked ubiquitination and degradation after viral infection. It also negatively regulates virus-triggered signaling by targeting MITA, also known as STING, for ubiquitination and degradation at the mitochondria. In addition, RNF5 determines breast cancer response to ER stress-inducing chemotherapies through the regulation of the L-glutamine carrier proteins SLC1A5 and SLC38A2 (SLC1A5/38A2). It also has been implicated in muscle organization and in recognition and processing of misfolded proteins. RNF5 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438401 [Multi-domain]  Cd Length: 54  Bit Score: 40.64  E-value: 2.48e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSyWSQSGPSGDySCPQCR 363
Cdd:cd16743      3 CNICLETARDAVVSLCGHLFCWPCLHQ-WLETRPERQ-ECPVCK 44
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 17-75 2.54e-04

Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or PAAD, is a subfamily of the Death Domain (DD) superfamily and it functions in several signaling pathways. The Pyrin domain is found at the N-terminus of a variety of proteins and serves as a linker that recruits other domains into signaling complexes. Pyrin-containing proteins include NALPs, ASC (Apoptosis-associated speck-like protein containing a CARD), and the interferon-inducible p200 (IFI-200) family of proteins which includes the human IFI-16, myeloid cell nuclear differentiation antigen (MNDA) and absent in melanoma (AIM) 2. NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. ASC and NALPs are involved in the regulation of inflammation. ASC, NALP1 and NALP3 are involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP12 functions as a negative regulator of inflammation. The p200 proteins are involved in the regulation of cell cycle and differentiation. 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 Caspase activation and recruitment domain (CARD) and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260019  Cd Length: 73  Bit Score: 41.14  E-value: 2.54e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899   17 LDNLTGAEFKRFKHYLQDQGQIAWGKLEKADTDDTVDLMVQVYSTGAG-DIILSILKTIK 75
Cdd:cd08305      5 LENITDEEFKMFKSLLASELKLTRKMQEEYDRIEIADLMEEKFGEDAGlDKLIEVFEDMP 64
RING-HC_PRT1-like cd23132
RING finger, HC subclass, found in Arabidopsis thaliana proteolysis 1 protein (PRT1) and ...
 316-363 2.65e-04

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


Pssm-ID: 438494 [Multi-domain]  Cd Length: 52  Bit Score: 40.48  E-value: 2.65e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2073512899  316 DQSRCGVCEQLLRDPVITTCGHSFCRQCIssYWSQSGpSGDYSCPQCR 363
Cdd:cd23132      1 EEFLCCICLDLLYKPVVLECGHVFCFWCV--HRCMNG-YDESHCPLCR 45
RING-HC_PML_C-V cd16579
RING finger, HC subclass, found in promyelocytic leukemia protein (PML) and similar proteins; ...
 314-363 2.83e-04

RING finger, HC subclass, found in promyelocytic leukemia protein (PML) and similar proteins; Protein PML, also known as RING finger protein 71 (RNF71) or tripartite motif-containing protein 19 (TRIM19), is predominantly a nuclear protein with a broad intrinsic antiviral activity. It is the eponymous component of PML nuclear bodies (PML NBs) and has been implicated in a wide variety of cell processes, including DNA damage signaling, apoptosis, and transcription. PML interferes with the replication of many unrelated viruses, including human immunodeficiency virus 1 (HIV-1), human foamy virus (HFV), poliovirus, influenza virus, rabies virus, EMCV, adeno-associated virus (AAV), and vesicular stomatitis virus (VSV). It also selectively interacts with misfolded proteins through distinct substrate recognition sites and conjugates these proteins with the small ubiquitin-like modifiers (SUMOs) through its SUMO ligase activity. PML belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 438241 [Multi-domain]  Cd Length: 52  Bit Score: 40.23  E-value: 2.83e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2073512899  314 TQDQSRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPSGDYSCPQCR 363
Cdd:cd16579      1 EFKFLRCPGCKAEYKCPKLLPCLHTVCSGCLEALAEQASETTEFQCPICK 50
RING-HC_RNF168 cd16550
RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; ...
 319-365 3.26e-04

RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; RNF168 is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. It, together with RNF8, functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates, such as H2A and H2AX with H2AK13/15 ubiquitylation, facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. Moreover, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF168 contains an N-terminal C3HC4-type RING-HC finger that catalyzes H2A-K15ub and interacts with H2A, and two MIU (motif interacting with ubiquitin) domains responsible for the interaction with K63 linked poly-ubiquitin.


Pssm-ID: 438212 [Multi-domain]  Cd Length: 48  Bit Score: 40.05  E-value: 3.26e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2073512899  319 RCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSgpsgDYSCPQCRKR 365
Cdd:cd16550      2 LCPICLEILVEPVTLPCNHTLCMPCFQSTVEKA----SLCCPLCRLR 44
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
 304-366 3.38e-04

RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 44.50  E-value: 3.38e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2073512899  304 SDPNVWRNVLTQDQsRCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPSgdySCPQCRKRS 366
Cdd:COG5574    203 SKKNGLPFIPLADY-KCFLCLEEPEVPSCTPCGHLFCLSCLLISWTKKKYE---FCPLCRAKV 261
RING-HC_RAD5 cd23131
RING finger, HC subclass, found in radiation sensitivity protein 5 (RAD5) and similar proteins; ...
 318-363 3.48e-04

RING finger, HC subclass, found in radiation sensitivity protein 5 (RAD5) and similar proteins; RAD5, also known as revertibility protein 2 (REV2), or DNA repair protein RAD5, is a probable helicase, and a member of the UBC2/RAD6 epistasis group. It functions with the DNA repair protein RAD18 in error-free postreplication DNA repair. It is involved in the maintenance of wild-type rates of instability of simple repetitive sequences such as poly(GT) repeats. It may also be involved in maintaining a balance which acts in favor of error-prone non-homologous joining during DNA double-strand breaks repairs. It recruits the UBC13-MMS2 dimer to chromatin for DNA repair. RAD5 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438493 [Multi-domain]  Cd Length: 65  Bit Score: 40.51  E-value: 3.48e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2073512899  318 SRCGVCEQLLRDP---VITTCGHSFCRQCISSYWS-QSGPSGDYSCPQCR 363
Cdd:cd23131      4 VECSICTQEPIEVgevVFTECGHSFCEDCLLEYIEfQNKKKLDLKCPNCR 53
RING-HC_TRIM13_C-V cd16762
RING finger, HC subclass, found in tripartite motif-containing protein 13 (TRIM13) and similar ...
 320-366 3.50e-04

RING finger, HC subclass, found in tripartite motif-containing protein 13 (TRIM13) and similar proteins; TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts with proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). It also targets the known ER proteolytic substrate CD3-delta, but not the N-end rule substrate Ub-R-YFP (yellow fluorescent protein) for degradation. Moreover, TRIM13 regulates ubiquitination and degradation of NEMO to suppress tumor necrosis factor (TNF) induced nuclear factor-kappaB (NF- kappa B) activation. It is also involved in NF-kappaB p65 activation and nuclear factor of activated T-cells (NFAT)-dependent activation of c-Rel upon T-cell receptor engagement. Furthermore, TRIM13 negatively regulates melanoma differentiation-associated gene 5 (MDA5)-mediated type I interferon production. It also regulates caspase-8 ubiquitination, translocation to autophagosomes, and activation during ER stress induced cell death. Meanwhile, TRIM13 enhances ionizing radiation-induced apoptosis by increasing p53 stability and decreasing AKT kinase activity through MDM2 and AKT degradation. TRIM13 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region. In addition, TRIM13 contains a C-terminal transmembrane domain.


Pssm-ID: 438418 [Multi-domain]  Cd Length: 56  Bit Score: 40.28  E-value: 3.50e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPS----GDYSCPQCRKRS 366
Cdd:cd16762      6 CPICCCLFDDPRVLPCSHNFCKKCLEGILEGNVRTmlwrPPFKCPTCRKET 56
SPRY cd11709
SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit ...
 1809-1929 3.90e-04

SPRY domain; SPRY domains, first identified in the SP1A kinase of Dictyostelium and rabbit Ryanodine receptor (hence the name), are homologous to B30.2. SPRY domains have been identified in at least 11 protein families, covering a wide range of functions, including regulation of cytokine signaling (SOCS), RNA metabolism (DDX1 and hnRNP), immunity to retroviruses (TRIM5alpha), intracellular calcium release (ryanodine receptors or RyR) and regulatory and developmental processes (HERC1 and Ash2L). B30.2 also contains residues in the N-terminus that form a distinct PRY domain structure; i.e. B30.2 domain consists of PRY and SPRY subdomains. B30.2 domains comprise the C-terminus of three protein families: BTNs (receptor glycoproteins of immunoglobulin superfamily); several TRIM proteins (composed of RING/B-box/coiled-coil or RBCC core); Stonutoxin (secreted poisonous protein of the stonefish Synanceia horrida). TRIM/RBCC proteins are involved in a variety of processes, including apoptosis, cell cycle regulation, cell growth, senescence, viral response, meiosis, cell differentiation, and vesicular transport. Genes belonging to this family are implicated in several human diseases that vary from cancer to rare genetic syndromes. The PRY-SPRY domain in these TRIM families is suggested to serve as the target binding site. While SPRY domains are evolutionarily ancient, B30.2 domains are a more recent adaptation where the SPRY/PRY combination is a possible component of immune defense. Mutations found in the SPRY-containing proteins have shown to cause Mediterranean fever and Opitz syndrome.


Pssm-ID: 293931  Cd Length: 118  Bit Score: 42.03  E-value: 3.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1809 GRCYWEAEW---SGDGAEIAVAYKSIKRkewSDESALGCNDKSWGLFCSPHGYYAKHNNEPTdiPVPSSRSSRVGVYLDW 1885
Cdd:cd11709      1 GKWYWEVRVdsgNGGLIQVGWATKSFSL---DGEGGVGDDEESWGYDGSRLRKGHGGSSGPG--GRPWKSGDVVGCLLDL 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1886 PAGTLSFY------SVFSDTLTHLhtfhstfTESLYPGFRVWPDSSVSLC 1929
Cdd:cd11709     76 DEGTLSFSlngkdlGVAFTNLFLK-------GGGLYPAVSLGSGQGVTIN 118
mRING-HC-C3HC3D_TRAF5 cd16642
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
 315-346 3.98e-04

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 5 (TRAF5) and similar proteins; TRAF5, also known as RING finger protein 84 (RNF84), is an important signal transducer for a wide range of TNF receptor superfamily members, including tumor necrosis factor receptor 1 (TNFR1), TNFR2, CD40, and other lymphocyte costimulatory receptors, RANK/TRANCE-R, ectodysplasin-A Receptor (EDAR), lymphotoxin-beta receptor (LT-betaR), latent membrane protein 1 (LMP1), and IRE1. It functions as an activator of NF-kappaB, MAPK, and JNK, and is involved in both RANKL- and TNFalpha-induced osteoclastogenesis. It mediates CD40 signaling by associating with the cytoplasmic tail of CD40. It also negatively regulates Toll-like receptor (TLR) signaling and functions as a negative regulator of the interleukin 6 (IL-6) receptor signaling pathway that limits the differentiation of inflammatory CD4(+) T cells. TRAF5 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain.


Pssm-ID: 438304 [Multi-domain]  Cd Length: 56  Bit Score: 40.11  E-value: 3.98e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2073512899  315 QDQSRCGVCEQLLRDPVITTCGHSFCRQCISS 346
Cdd:cd16642      2 EDRYKCATCHFVLHNPHQTGCGHRFCQHCILS 33
RING-HC_RNF169 cd16551
RING finger, HC subclass, found in RING finger protein 169 (RNF169) and similar proteins; ...
 317-365 4.75e-04

RING finger, HC subclass, found in RING finger protein 169 (RNF169) and similar proteins; RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to regulation of the DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. RNF169 contains an N-terminal C3HC4-type RING-HC finger and a C-terminal MIU (motif interacting with ubiquitin) domain.


Pssm-ID: 438213 [Multi-domain]  Cd Length: 55  Bit Score: 39.84  E-value: 4.75e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2073512899  317 QSRCGVCEQLLRDPVITTCGHSFCRQCISSYW--SQSGPsgdySCPQCRKR 365
Cdd:cd16551      1 ELTCAGCLEVPVEPATLPCGHTLCRGCANRALdaAEAGP----TCPRCRAP 47
SPRY_SOCS3 cd12876
SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY ...
 1840-1893 5.25e-04

SPRY domain in the suppressor of cytokine signaling 3 (SOCS3) family; The SPRY domain-containing SOCS box protein family (SPSB1-4, also known as SSB-1 to -4) is composed of a central SPRY protein interaction domain and a C-terminal SOCS box. All four SPSB proteins interact with c-Met, the hepatocyte growth factor receptor, but SOCS3 regulates cellular response to a variety of cytokines such as leukemia inhibitory factor (LIF) and interleukin 6. SOCS3, along with SOCS1, are expressed by immune cells and cells of the central nervous system (CNS) and have the potential to impact immune processes within the CNS. In non-small cell lung cancer (NSCLC), SOCS3 is silenced and proline-rich tyrosine kinase 2 (Pyk2) is over-expressed; it has been suggested that SOCS3 could be an effective way to prevent the progression of NSCLC due to its role in regulating Pyk2 expression.


Pssm-ID: 293936  Cd Length: 185  Bit Score: 42.92  E-value: 5.25e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2073512899 1840 SALGCNDKSWGLfcSPHGYyAKHNNEPTDIPVP-SSRSSRVGVYLDWPAGTLSFY 1893
Cdd:cd12876     81 SLLGEDEESWGL--SYKGL-LWHDGQSRPYTSPfGNQGTIIGVHLDMWRGTLTFY 132
RING-HC_RNFT2 cd16742
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2 ...
 320-363 5.28e-04

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2(RNFT2); RNFT2, also known as transmembrane protein 118 (TMEM118), is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear.


Pssm-ID: 438400 [Multi-domain]  Cd Length: 67  Bit Score: 40.25  E-value: 5.28e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQsgpsgDYSCPQCR 363
Cdd:cd16742     16 CAICQAEFREPLILICQHVFCEECLCLWFDR-----ERTCPLCR 54
RING-HC_RNF151 cd16547
RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins; ...
 320-364 5.42e-04

RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins; RNF151 is a testis-specific RING finger protein that interacts with dysbindin, a synaptic and microtubular protein that binds brain snapin, a SNARE-binding protein that mediates intracellular membrane fusion in both neuronal and non-neuronal cells. Thus, it may be involved in acrosome formation of spermatids by interacting with multiple proteins participating in membrane biogenesis and microtubule organization. RNF151 contains a C3HC4-type RING finger domain, a putative nuclear localization signal (NLS), and a TNF receptor associated factor (TRAF)-type zinc finger domain.


Pssm-ID: 438209 [Multi-domain]  Cd Length: 49  Bit Score: 39.37  E-value: 5.42e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSgpsgdYSCPQCRK 364
Cdd:cd16547      6 CSICHGVLRCPVRLSCSHIFCKKCILQWLKRQ-----ETCPCCRK 45
RING-HC_TRIM59_C-V cd16763
RING finger, HC subclass, found in tripartite motif-containing protein 59 (TRIM59) and similar ...
 320-363 5.81e-04

RING finger, HC subclass, found in tripartite motif-containing protein 59 (TRIM59) and similar proteins; TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis. It is upregulated in gastric cancer and promotes gastric carcinogenesis by interacting with and targeting the P53 tumor suppressor for its ubiquitination and degradation. It also acts as a novel accessory molecule involved in cytotoxicity of BCG-activated macrophages (BAM). Moreover, TRIM59 may serve as a multifunctional regulator for innate immune signaling pathways. It interacts with ECSIT and negatively regulates nuclear factor-kappaB (NF- kappa B) and interferon regulatory factor (IRF)-3/7-mediated signal pathways. TRIM59 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region. In addition, TRIM59 contains a C-terminal transmembrane domain.


Pssm-ID: 438419 [Multi-domain]  Cd Length: 56  Bit Score: 39.51  E-value: 5.81e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPSGDY-------SCPQCR 363
Cdd:cd16763      6 CSVCYSLFEDPRVLPCSHTFCRNCLENILQVSGNFSIWrplrpplKCPNCR 56
RING-HC_RNF166 cd16549
RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins; ...
 317-363 6.09e-04

RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins; RNF166 is encoded by the gene RNF166 targeted by thyroid hormone receptor alpha1 (TRalpha1), which is important in brain development. It plays an important role in RNA virus-induced interferon-beta production by enhancing the ubiquitination of TRAF3 and TRAF6. RNF166, together with three closely related proteins: RNF114, RNF125 and RNF138, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 438211 [Multi-domain]  Cd Length: 47  Bit Score: 39.41  E-value: 6.09e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2073512899  317 QSRCGVCEQLLRDPV-ITTCGHSFCRQCISSYWSQSGPsgdySCPQCR 363
Cdd:cd16549      1 QFSCPICLEVYHKPVvITSCGHTFCGECLQPCLQVASP----LCPLCR 44
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 180-306 6.21e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 6.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899  180 NMSQIGRGPSSSDKPQTHRPVSPVPSCVSMKSDWSMGRPPNFSSGPPQSDPKPQTHR---PVSPVPSCVSMKS------- 249
Cdd:PHA03307    63 DRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPtppPASPPPSPAPDLSemlrpvg 142

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2073512899  250 -----DRSMGRPPNFSNGPPQSDPK------------PQTHRPVSPVPSCVSMKSDRSMGRPPNFSNGPPQSDP 306
Cdd:PHA03307   143 spgppPAASPPAAGASPAAVASDAAssrqaalplsspEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISAS 216
mRING-HC-C3HC3D_TRAF4 cd16641
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
 320-361 8.08e-04

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 4 (TRAF4) and similar proteins; TRAF4, also known as cysteine-rich domain associated with RING and Traf domains protein 1, metastatic lymph node gene 62 protein (MLN 62), or RING finger protein 83 (RNF83), is a member of the TRAF protein family, which mainly function in the immune system, where they mediate signaling through tumor necrosis factor receptors (TNFRs) and interleukin-1/Toll-like receptors (IL-1/TLRs). It also plays a critical role in nervous system, as well as in carcinogenesis. TRAF4 promotes the growth and invasion of colon cancer through the Wnt/beta-catenin pathway. It contributes to the TNFalpha-induced activation of the 70 kDa ribosomal protein S6 kinase (p70s6k) signaling pathway, and activation of transforming growth factor beta (TGF-beta)-induced SMAD-dependent signaling and non-SMAD signaling in breast cancer. It also enhances osteosarcoma cell proliferation and invasion by the Akt signaling pathway. Moreover, TRAF4 is a novel phosphoinositide-binding protein modulating tight junctions and favoring cell migration. TRAF4 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain.


Pssm-ID: 438303 [Multi-domain]  Cd Length: 45  Bit Score: 38.97  E-value: 8.08e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2073512899  320 CGVCEQLLRDPV-ITTCGHSFCRQCISSYWSQsgpsGDYSCPQ 361
Cdd:cd16641      4 CPLCRLPMREPVqISTCGHRFCDTCLQEFLSE----GVFKCPE 42
RING-HC_RNF185 cd16744
RING finger, HC subclass, found in RING finger protein 185 (RNF185) and similar proteins; ...
 320-363 8.41e-04

RING finger, HC subclass, found in RING finger protein 185 (RNF185) and similar proteins; RNF185 is an E3 ubiquitin-protein ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR). It controls the degradation of CFTR and CFTR F508del allele in a RING- and proteasome-dependent manner, but does not control that of other classical ERAD model substrates. It also negatively regulates osteogenic differentiation by targeting dishevelled2 (Dvl2), a key mediator of the Wnt signaling pathway, for degradation. Moreover, RNF185 regulates selective mitochondrial autophagy through interaction with the Bcl-2 family protein BNIP1. It also plays an important role in cell adhesion and migration through the modulation of cell migration by ubiquitinating paxillin. RNF185 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438402 [Multi-domain]  Cd Length: 57  Bit Score: 39.14  E-value: 8.41e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSyWSQSGPSgDYSCPQCR 363
Cdd:cd16744      3 CNICLDTAKDAVVSLCGHLFCWPCLHQ-WLETRPN-RQVCPVCK 44
RING-HC_RAD18 cd16529
RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; ...
 319-364 9.04e-04

RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; RAD18, also known as HR18 or RING finger protein 73 (RNF73), is an E3 ubiquitin-protein ligase involved in post replication repair of UV-damaged DNA via its recruitment to stalled replication forks. It associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on K164. It also interacts with another E2 ubiquitin conjugating enzyme RAD6 to form a complex that monoubiquitinates proliferating cell nuclear antigen at stalled replication forks in DNA translesion synthesis. Moreover, Rad18 is a key factor in double-strand break DNA damage response (DDR) pathways via its association with K63-linked polyubiquitylated chromatin proteins. It can function as a mediator for DNA damage response signals to activate the G2/M checkpoint in order to maintain genome integrity and cell survival after ionizing radiation (IR) exposure. RAD18 contains a C3HC4-type RING-HC finger, a ubiquitin-binding zinc finger domain (UBZ), a SAP (SAF-A/B, Acinus and PIAS) domain, and a RAD6-binding domain (R6BD).


Pssm-ID: 438192 [Multi-domain]  Cd Length: 54  Bit Score: 38.82  E-value: 9.04e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2073512899  319 RCGVCEQLLR-DPVITTCGHSFCRQCISSYWSQsgpsgDYSCPQCRK 364
Cdd:cd16529      6 RCPICFEYFNtAMMITQCSHNYCSLCIRRFLSY-----KTQCPTCRA 47
RING-HC_TRIM50_like_C-IV cd16605
RING finger, HC subclass, found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 ...
 320-364 1.07e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 and similar proteins; TRIM50 is a stomach-specific E3 ubiquitin-protein ligase, encoded by the Williams-Beuren syndrome (WBS) TRIM50 gene, which regulates vesicular trafficking for acid secretion in gastric parietal cells. It colocalizes, interacts with, and increases the level of p62/SQSTM1, a multifunctional adaptor protein implicated in various cellular processes including the autophagy clearance of polyubiquitinated protein aggregates. It also promotes the formation and clearance of aggresome-associated polyubiquitinated proteins through the interaction with histone deacetylase 6 (HDAC6), a tubulin specific deacetylase that regulates microtubule-dependent aggresome formation. TRIM50 can be acetylated by PCAF and p300. TRIM50 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. This subfamily also includes two paralogs of TRIM50, tripartite motif-containing protein 73 (TRIM73), also known as tripartite motif-containing protein 50B (TRIM50B), and tripartite motif-containing protein 74 (TRIM74), also known as tripartite motif-containing protein 50C (TRIM50C), both of which are WBS-related genes encoding proteins that may also act as E3 ligases. In contrast with TRIM50, TRIM73 and TRIM74 belong to the C-V subclass of TRIM family of proteins that are defined by N-terminal RBCC domains only.


Pssm-ID: 438267 [Multi-domain]  Cd Length: 45  Bit Score: 38.58  E-value: 1.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCIssyWSQSGP-SGDYSCPQCRK 364
Cdd:cd16605      3 CPICLEVFKEPLMLQCGHSYCKSCL---VSLSGElDGQLLCPVCRQ 45
RING-HC_RING1 cd16739
RING finger, HC subclass, found in really interesting new gene 1 protein (RING1) and similar ...
 315-375 1.26e-03

RING finger, HC subclass, found in really interesting new gene 1 protein (RING1) and similar proteins; RING1, also known as polycomb complex protein RING1, RING finger protein 1 (RNF1), or RING finger protein 1A (RING1A), was identified as a transcriptional repressor that is associated with the Polycomb group (PcG) protein complex involved in stable repression of gene activity. It is a core component of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase that transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. RING1 interacts with multiple PcG proteins and displays tumorigenic activity. It also shows zinc-dependent DNA binding activity. Moreover, RING1 inhibits transactivation of the DNA-binding protein recombination signal binding protein-Jkappa (RBP-J) by Notch through interaction with the LIM domains of KyoT2. RING1 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438397 [Multi-domain]  Cd Length: 70  Bit Score: 39.29  E-value: 1.26e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2073512899  315 QDQSRCGVCEQLLRDPVITT-CGHSFCRQCISSYWSqsgpSGDYSCPQCRKRSRAQPSLNPD 375
Cdd:cd16739      1 HSELMCPICLDMLKNTMTTKeCLHRFCSDCIVTALR----SGNKECPTCRKKLVSKRSLRPD 58
RING-HC_KEG-like cd23140
RING finger, HC subclass, found in Arabidopsis thaliana protein KEEP ON GOING (KEG) and ...
 320-366 1.26e-03

RING finger, HC subclass, found in Arabidopsis thaliana protein KEEP ON GOING (KEG) and similar proteins; KEG, also called RING-type E3 ubiquitin transferase KEG, is a RING E3 ubiquitin-protein ligase that mediates E2-dependent protein ubiquitination. It is essential for Arabidopsis growth and development. It acts as a negative regulator of abscisic acid signaling. It is required for ABSCISIC ACID-INSENSITIVE5 (ABI5) degradation, by mediating its ubiquitination. Together with EDR1, KEG may regulate endocytic trafficking and/or the formation of signaling complexes on trans-Golgi network (TGN)/ early endosome (EE) vesicles during stress responses. KEG is a multidomain protein that includes a C3HC4-type RING-HC finger, a kinase domain, ankyrin repeats, and 12 HERC2-like (for HECT and RCC1-like) repeats.


Pssm-ID: 438502 [Multi-domain]  Cd Length: 57  Bit Score: 38.78  E-value: 1.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2073512899  320 CGVC----EQLLRDPVITTCGHSFCRQCISSYWSQSGPSgDYSCPQCRKRS 366
Cdd:cd23140      4 CSVCsegyNEDERVPLLLQCGHTFCKDCLSQMFIRCTDL-TLKCPRCRQSV 53
zf-RING_2 pfam13639
Ring finger domain;
320-363 1.45e-03

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 38.16  E-value: 1.45e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2073512899  320 CGVCEQLL---RDPVITTCGHSFCRQCISSyWSQSGPsgdySCPQCR 363
Cdd:pfam13639    3 CPICLEEFeegDKVVVLPCGHHFHRECLDK-WLRSSN----TCPLCR 44
RING-HC_MuRF1 cd16759
RING finger, HC subclass, found in muscle-specific RING finger protein 1 (MuRF-1) and similar ...
 315-363 1.51e-03

RING finger, HC subclass, found in muscle-specific RING finger protein 1 (MuRF-1) and similar proteins; MuRF-1, also known as tripartite motif-containing protein 63 (TRIM63), RING finger protein 28 (RNF28), iris RING finger protein, or striated muscle RING zinc finger, is an E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover. It is predominantly fast (type II) fibre-associated in skeletal muscle and can bind to many myofibrillar proteins, including titin, nebulin, the nebulin-related protein NRAP, troponin-I (TnI), troponin-T (TnT), myosin light chain 2 (MLC-2), myotilin, and T-cap. The early and robust upregulation of MuRF-1 is triggered by disuse, denervation, starvation, sepsis, or steroid administration resulting in skeletal muscle atrophy. It also plays a role in maintaining titin M-line integrity. It associates with the periphery of the M-line lattice and may be involved in the regulation of the titin kinase domain. It also participates in muscle stress response pathways and gene expression. MuRF-1 belongs to the C-II subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains.


Pssm-ID: 319673 [Multi-domain]  Cd Length: 63  Bit Score: 38.86  E-value: 1.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2073512899  315 QDQSRCGVCEQLLRDPV-ITTCGHSFCRQCISS-------YWSQSGPS-----GDYSCPQCR 363
Cdd:cd16759      1 EKQLICPICLEMFTKPVvILPCQHNLCRKCANDifqaanpYWQSRGTSmlgsgGRFRCPSCR 62
RING-HC_ORTHRUS_rpt2 cd23139
second RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; ...
 320-364 1.60e-03

second RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; This subfamily includes Arabidopsis thaliana ORTHRUS 1-5. They are E3 ubiquitin-protein ligases that may participate in CpG methylation-dependent transcriptional regulation and/or epigenetic transcriptional silencing. ORTHRUS 1 mediates ubiquitination with the E2 ubiquitin-conjugating enzymes UBC11, UBC8 and UBC8 homologs (e.g. UBC10, UBC11, UBC28 and UBC29) but not with UBC27, UBC30, UBC32, UBC34 and UBC36. ORTHRUS 2 and 5 mediate ubiquitination with the E2 ubiquitin-conjugating enzyme UBC11. ORTHRUS 1 and 2 promote methylation-mediated gene silencing leading, for example, to early flowering. They can bind to CpG, CpNpG, and CpNpN DNA motifs, with a strong preference for methylated forms, and with highest affinity for CpG substrates. Members of this subfamily contain two typical C3HC4-type RING-HC fingers. This model corresponds to the second one.


Pssm-ID: 438501 [Multi-domain]  Cd Length: 72  Bit Score: 38.98  E-value: 1.60e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYW-----SQSGPSGDYS---------CPQCRK 364
Cdd:cd23139      8 CQICKKVLSLPVSTPCGHNFCKACLEAKFagiadVRDRGNGGRSlrarknvkpCPCCKT 66
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 1493-1688 1.72e-03

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 41.93  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1493 DLQQSGEMLLSALQSPNC-KLETLRLTGCKL-TGRFLALTLQGAnPHLRELDISDgelqysggellhqplnqdckvrliC 1570
Cdd:cd09293     34 ELYMCPISDPPLDQLSNCnKLKKLILPGSKLiDDEGLIALAQSC-PNLQVLDLRA------------------------C 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1571 CRLKDSScaVMASVLQfCvSQLSVLDM---TGCDLQTSdeKLLSCLGNPNCQLKTLKLADCKLTEESCKALAStlQSSVS 1647
Cdd:cd09293     89 ENITDSG--IVALATN-C-PKLQTINLgrhRNGHLITD--VSLSALGKNCTFLQTVGFAGCDVTDKGVWELAS--GCSKS 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2073512899 1648 LTELDLTN-SELKDSGIQLLSAGLSNPHckLQTLRLSGC-LIT 1688
Cdd:cd09293    161 LERLSLNNcRNLTDQSIPAILASNYFPN--LSVLEFRGCpLIT 201
RING-HC_GEFO-like cd16507
RING finger, HC subclass, found in Dictyostelium discoideum Ras guanine nucleotide exchange ...
 320-363 1.91e-03

RING finger, HC subclass, found in Dictyostelium discoideum Ras guanine nucleotide exchange factor O (RasGEFO) and similar proteins; RasGEFO, also known as RasGEF domain-containing protein O, functions as a Ras guanine-nucleotide exchange factor (RasGEFs), activating Ras by catalyzing the replacement of GDP with GTP. RasGEFs are particularly important for signaling in development and chemotaxis in many organisms, including Dictyostelium. RasGEFO contains a C3HC4-type RING-HC finger that may be responsible for E3 ubiquitin ligase activity.


Pssm-ID: 438170 [Multi-domain]  Cd Length: 58  Bit Score: 38.10  E-value: 1.91e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2073512899  320 CGVCEQLLRDP-VITTCGHSFCRQCISSywSQSGPsgdySCPQCR 363
Cdd:cd16507     12 CGICQNLFKDPnTLIPCGHAFCLDCLTT--NASIK----NCIQCK 50
RING-HC_RING2 cd16740
RING finger, HC subclass, found in really interesting new gene 2 protein (RING2) and similar ...
 320-375 1.95e-03

RING finger, HC subclass, found in really interesting new gene 2 protein (RING2) and similar proteins; RING2, also known as huntingtin-interacting protein 2-interacting protein 3, HIP2-interacting protein 3, protein DinG, RING finger protein 1B (RING1B), RING finger protein 2 (RNF2), or RING finger protein BAP-1, is an E3 ubiquitin-protein ligase that interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve the specific monoubiquitination of K119 on histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation. RING2 is a core component of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. The enzymatic activity of RING2 is enhanced by the interaction with BMI1/PCGF4, and it is dispensable for early embryonic development and much of the gene repression activity of PRC1. Moreover, RING2 plays a key role in terminating neural precursor cell (NPC)-mediated production of subcerebral projection neurons (SCPNs) during neocortical development. It also plays a critical role in nonhomologous end-joining (NHEJ)-mediated end-to-end chromosome fusions. Furthermore, RING2 is essential for expansion of hepatic stem/progenitor cells. It promotes hepatic stem/progenitor cell expansion through simultaneous suppression of cyclin-dependent kinase inhibitors (CDKIs) Cdkn1a and Cdkn2a, known negative regulators of cell proliferation. RING2 also negatively regulates p53 expression through directly binding with both p53 and MDM2 and promoting MDM2-mediated p53 ubiquitination in selective cancer cell types to stimulate tumor development. RING2 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438398 [Multi-domain]  Cd Length: 77  Bit Score: 38.92  E-value: 1.95e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2073512899  320 CGVCEQLLRDPVITT-CGHSFCRQCISSYWSqsgpSGDYSCPQCRKRSRAQPSLNPD 375
Cdd:cd16740     15 CPICLDMLKNTMTTKeCLHRFCADCIITALR----SGNKECPTCRKKLVSKRSLRPD 67
RING-HC_MmTRIM43-like cd23133
RING finger, HC subclass, found in Mus musculus tripartite motif-containing protein 43 (TRIM43) ...
 320-364 2.06e-03

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


Pssm-ID: 438495 [Multi-domain]  Cd Length: 57  Bit Score: 37.97  E-value: 2.06e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCIssYWSQSGPSGDYSCPQCRK 364
Cdd:cd23133      6 CSICQGIFMNPVYLRCGHKFCEACL--LLFQEDIKFPAYCPMCRQ 48
RING-HC_MID2 cd16754
RING finger, HC subclass, found in midline-2 (MID2) and similar proteins; MID2, also known as ...
 320-363 2.34e-03

RING finger, HC subclass, found in midline-2 (MID2) and similar proteins; MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is a probable E3 ubiquitin-protein ligase and is highly related to MID1 that associates with cytoplasmic microtubules along their length and throughout the cell cycle. Like MID1, MID2 associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. MID2 can also substitute for MID1 to control exocytosis of lytic granules in cytotoxic T cells. Loss-of-function mutations in MID2 lead to the human X-linked intellectual disability (XLID). MID2 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxy-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. MID2 hetero-dimerizes in vitro with its paralog MID1.


Pssm-ID: 438412 [Multi-domain]  Cd Length: 70  Bit Score: 38.43  E-value: 2.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPSGD-------YSCPQCR 363
Cdd:cd16754     10 CPICLELFEDPLLLPCAHSLCFSCAHRILTSGCASGEsieppsaFQCPTCR 60
RING-HC_TRIM2_like_C-VII cd16586
RING finger, HC subclass, found in tripartite motif-containing protein TRIM2, TRIM3, and ...
 320-363 2.51e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM2, TRIM3, and similar proteins; TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It also plays an important role in the central nervous system (CNS). In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. Both TRIM2 and TRIM3 belong to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438248 [Multi-domain]  Cd Length: 45  Bit Score: 37.43  E-value: 2.51e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSgpSGDYSCPQCR 363
Cdd:cd16586      4 CGICLERYKNPKVLPCLHTFCERCLQNYIPAE--SLSLSCPVCR 45
mRING-HC-C4C4_TRIM37_C-VIII cd16619
Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 ...
 319-363 2.52e-03

Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 (TRIM37) and similar proteins; TRIM37, also known as mulibrey nanism protein, or MUL, is a peroxisomal E3 ubiquitin-protein ligase that is involved in the tumorigenesis of several cancer types, including pancreatic ductal adenocarcinoma (PDAC), hepatocellular carcinoma (HCC), breast cancer, and sporadic fibrothecoma. It mono-ubiquitinates histone H2A, a chromatin modification associated with transcriptional repression. Moreover, TRIM37 possesses anti-HIV-1 activity, and interferes with viral DNA synthesis. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction, and hepatomegaly. TRIM37 belongs to the C-VIII subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a MATH (meprin and TRAF-C homology) domain positioned C-terminal to the RBCC domain. Its MATH domain has been shown to interact with the TRAF (TNF-Receptor-Associated Factor) domain of six known TRAFs in vitro.


Pssm-ID: 438281 [Multi-domain]  Cd Length: 43  Bit Score: 37.34  E-value: 2.52e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2073512899  319 RCGVCEQLLRDPVI-TTCGHSFCRQCISSYWSQSGPsgdySCPQCR 363
Cdd:cd16619      2 RCFICMEKLRDPRLcPHCSKLFCKGCIRRWLSEQRS----SCPHCR 43
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
1617-1644 2.87e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 37.00  E-value: 2.87e-03
                            10        20
                    ....*....|....*....|....*...
gi 2073512899  1617 NCQLKTLKLADCKLTEESCKALASTLQS 1644
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
RING-HC_RNF8 cd16535
RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is ...
 320-365 3.18e-03

RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal forkhead-associated (FHA) domain and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438197 [Multi-domain]  Cd Length: 64  Bit Score: 37.76  E-value: 3.18e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSyWSQSgpsgDYSCPQCRKR 365
Cdd:cd16535      4 CSICSELFIEAVTLNCSHSFCSYCITE-WMKR----KKECPICRKP 44
RING-HC_Topors cd16574
RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein ...
 318-365 4.34e-03

RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein (Topors) and similar proteins; Topors, also known as topoisomerase I-binding RING finger protein, tumor suppressor p53- binding protein 3, or p53-binding protein 3 (p53BP3), is a ubiquitously expressed nuclear E3 ubiquitin-protein ligase that can ligate both ubiquitin and small ubiquitin-like modifier (SUMO) to substrate proteins in the nucleus. It contains an N-terminal C3HC4-type RING-HC finger which ligates ubiquitin to its target proteins including DNA topoisomerase I, p53, NKX3.1, H2AX, and the AAV-2 Rep78/68 proteins. As a RING-dependent E3 ubiquitin ligase, Topors works with the E2 enzymes UbcH5a, UbcH5c, and UbcH6, but not with UbcH7, CDC34, or UbcH2b. Topors acts as a tumor suppressor in various malignancies. It regulates p53 modification, suggesting it may be responsible for astrocyte elevated gene-1 (AEG-1, also known as metadherin, or LYRIC) ubiquitin modification. Plk1-mediated phosphorylation of Topors inhibits Topors-mediated sumoylation of p53, whereas p53 ubiquitination is enhanced, leading to p53 degradation. It also functions as a negative regulator of the prostate tumor suppressor NKX3.1. Moreover, Topors is associated with promyelocytic leukemia nuclear bodies, and may be involved in the cellular response to camptothecin. It also plays a key role in the turnover of H2AX protein, discriminating the type of DNA damaging stress. Furthermore, Topors is a cilia-centrosomal protein associated with autosomal dominant retinal degeneration. Mutations in TOPORS cause autosomal dominant retinitis pigmentosa (adRP).


Pssm-ID: 438236 [Multi-domain]  Cd Length: 47  Bit Score: 36.88  E-value: 4.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2073512899  318 SRCGVCEQLLRDP--VITTCGHSFCRQCISSyWSQSGPsgdySCPQCRKR 365
Cdd:cd16574      2 SSCPICLDRFENEkaFLDGCFHAFCFTCILE-WSKVKN----ECPLCKQP 46
RING-HC_MuRF2 cd16760
RING finger, HC subclass, found in muscle-specific RING finger protein 2 (MuRF-2) and similar ...
 315-363 4.93e-03

RING finger, HC subclass, found in muscle-specific RING finger protein 2 (MuRF-2) and similar proteins; MuRF-2, also known as tripartite motif-containing protein 55 (TRIM55) or RING finger protein 29 (RNF29), is a muscle-specific E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover and is also a ligand of the transactivation domain of the serum response transcription factor (SRF). It is predominantly slow-fibre associated and highly expressed in embryonic skeletal muscle. MuRF-2 associates transiently with microtubules, myosin, and titin during sarcomere assembly. It has been implicated in microtubule, intermediate filament, and sarcomeric M-line maintenance in striated muscle development, as well as in signaling from the sarcomere to the nucleus. It plays an important role in the earliest stages of skeletal muscle differentiation and myofibrillogenesis. It is developmentally downregulated and is assembled at the M-line region of the sarcomere and with microtubules. MuRF-2 belongs to the C-II subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains.


Pssm-ID: 438417 [Multi-domain]  Cd Length: 64  Bit Score: 37.28  E-value: 4.93e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2073512899  315 QDQSRCGVCEQLLRDPV-ITTCGHSFCRQCISSYWSQSGP------------SGDYSCPQCR 363
Cdd:cd16760      1 EKQLICPICLEMFTKPVvILPCQHNLCRKCANDIFQASNPylptrggttvasGGRFRCPSCR 62
RING-HC_UHRF2 cd16770
RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing ...
 320-363 5.56e-03

RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing protein 2 (UHRF2); UHRF2, also known as Np95/ICBP90-like RING finger protein (NIRF), Np95-like RING finger protein, nuclear protein 97, nuclear zinc finger protein Np97, RING finger protein 107, or E3 ubiquitin-protein ligase UHRF2, was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation, but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) through interacting with HBV core protein and promoting its degradation. UHRF2 contains an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) domain, a SET- and RING-associated (SRA) domain, and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438426 [Multi-domain]  Cd Length: 65  Bit Score: 37.10  E-value: 5.56e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISsywsQSGPSGDYSCPQCR 363
Cdd:cd16770      6 CICCQELVYQPVTTECQHNVCKSCLQ----RSFKAEVYTCPACR 45
PLN03208 PLN03208
E3 ubiquitin-protein ligase RMA2; Provisional
 320-354 5.57e-03

E3 ubiquitin-protein ligase RMA2; Provisional


Pssm-ID: 178747 [Multi-domain]  Cd Length: 193  Bit Score: 40.07  E-value: 5.57e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPS 354
Cdd:PLN03208    21 CNICLDQVRDPVVTLCGHLFCWPCIHKWTYASNNS 55
RING-HC_IRC20-like cd23135
RING finger, HC subclass, found in Saccharomyces cerevisiae increased recombination centers ...
 320-363 5.74e-03

RING finger, HC subclass, found in Saccharomyces cerevisiae increased recombination centers protein 20 (IRC20) and similar proteins; IRC20 is an uncharacterized ATP-dependent helicase that is probably involved in a pathway contributing to genomic integrity. IRC20 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438497 [Multi-domain]  Cd Length: 44  Bit Score: 36.34  E-value: 5.74e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGpsgdySCPQCR 363
Cdd:cd23135      6 CSICFSEIRSGAILKCGHFFCLSCIASWLREKS-----TCPLCK 44
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 139-194 6.12e-03

Fish-specific NACHT associated domain; This domain is frequently found associated with the NACHT domain (pfam05729) in fish and other vertebrates.


Pssm-ID: 464185 [Multi-domain]  Cd Length: 72  Bit Score: 37.21  E-value: 6.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2073512899  139 LQEHLKQRFSVVH----QESGVSSVQDIYTDLHIVEGRTGEVST-NNMSQIG---RGPSSSDKP 194
Cdd:pfam14484    1 LKSNLKKKFQCIFegnaKGGESTLLNEIYTELYITEGESGEVNEeHEVRQIEaasKKPESEETP 64
RING-HC_UHRF1 cd16769
RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing ...
 320-363 6.51e-03

RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing protein 1 (UHRF1); UHRF1, also known as inverted CCAAT box-binding protein of 90 kDa, nuclear protein 95, nuclear zinc finger protein Np95 (Np95), RING finger protein 106, transcription factor ICBP90, or E3 ubiquitin-protein ligase UHRF1, is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma (LSCC), gastric cancer (GC), esophageal squamous cell carcinoma (ESCC), colorectal cancer, prostate cancer, and breast cancer. UHRF1 can acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumor suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also a N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF1 contains an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) domain, a SET and RING finger associated (SRA) domain, and a C-terminal C3HC4-type RING-HC finger. It specifically binds to hemimethylated DNA, double-stranded CpG dinucleotides, and recruits the maintenance methyltransferase DNMT1 to its hemimethylated DNA substrate through its SRA domain. UHRF1-dependent H3K23 ubiquitylation has an essential role in maintenance DNA methylation and replication. The tandem Tudor domain directs UHRF1 binding to the heterochromatin mark histone H3K9me3 and the PHD domain targets UHRF1 to unmodified histone H3 in euchromatic regions. The RING-HC finger exhibits both autocatalytic E3 ubiquitin (Ub) ligase activity and activity against histone H3 and DNMT1.


Pssm-ID: 438425 [Multi-domain]  Cd Length: 84  Bit Score: 37.72  E-value: 6.51e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  320 CGVCEQLLRDPVITTCGHSFCRQCIssywSQSGPSGDYSCPQCR 363
Cdd:cd16769     15 CICCQELVFRPITTVCQHNVCKDCL----DRSFRAQVFSCPACR 54
RING-H2 cd16448
H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ...
 320-363 6.96e-03

H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). This family corresponds to the H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 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 serves as a scaffold 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: 438112 [Multi-domain]  Cd Length: 43  Bit Score: 36.23  E-value: 6.96e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2073512899  320 CGVCEQLLRDP---VITTCGHSFCRQCISSyWSQsgpSGDYSCPQCR 363
Cdd:cd16448      1 CVICLEEFEEGdvvRLLPCGHVFHLACILR-WLE---SGNNTCPLCR 43
RING-HC_TRAF3 cd16640
RING finger, HC subclass, found in tumor necrosis factor (TNF) receptor-associated factor 3 ...
 319-362 8.03e-03

RING finger, HC subclass, found in tumor necrosis factor (TNF) receptor-associated factor 3 (TRAF3) and similar proteins; TRAF3, also known as CAP-1, CD40 receptor-associated factor 1 (CRAF1), CD40-binding protein (CD40BP), or LMP1-associated protein 1 (LAP1), is a member of the TRAF protein family, which mainly functions in the immune system, where it mediates signaling through tumor necrosis factor receptors (TNFRs) and interleukin-1/Toll-like receptors (IL-1/TLRs). It also plays a unique cell type-specific and critical role in the restraint of B-cell homeostatic survival, a role with important implications for both B-cell differentiation and the pathogenesis of B-cell malignancies. TRAF3 differentially regulates differentiation of specific T cell subsets. It is required for iNKT cell development, restrains Treg cell development in the thymus, and plays an essential role in the homeostasis of central memory CD8+ T cells. TRAF3 contains an N-terminal domain with a typical C3HC4-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain, and a conserved TRAF-C domain.


Pssm-ID: 438302 [Multi-domain]  Cd Length: 42  Bit Score: 36.03  E-value: 8.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2073512899  319 RCGVCEQLLRDPVITTCGHSFCRQCISSYWSQSGPsgdySCPQC 362
Cdd:cd16640      2 KCEKCRLVLCNPKQTECGHRFCESCMNALLSSSNP----QCPAC 41
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 1298-1472 8.23e-03

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 40.00  E-value: 8.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1298 CAVVASVL--QFCVSQLSDLDMSGCDPQTSVEKLLSSLGNPNcrLKILRLKGC-KLTHESCKVVAS---FLQSANplLEL 1371
Cdd:cd09293     38 CPISDPPLdqLSNCNKLKKLILPGSKLIDDEGLIALAQSCPN--LQVLDLRACeNITDSGIVALATncpKLQTIN--LGR 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2073512899 1372 DLSNNVLRDSGVQLLSKGlsspHCKLQTLRLTDCHISDDGYVCLALTLMANpscVKELDLSN-NNSGESAKNLLFATLKD 1450
Cdd:cd09293    114 HRNGHLITDVSLSALGKN----CTFLQTVGFAGCDVTDKGVWELASGCSKS---LERLSLNNcRNLTDQSIPAILASNYF 186

                          170       180
                   ....*....|....*....|...
gi 2073512899 1451 PHLKMEELRlaGC-KLTERSYEI 1472
Cdd:cd09293    187 PNLSVLEFR--GCpLITDFSRII 207
RING-H2_Vps11 cd16688
RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 11 homolog ...
 318-365 8.58e-03

RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 11 homolog (Vps11) and similar proteins; Vps11, also known as RING finger protein 108 (RNF108), is a soluble protein involved in regulation of glycolipid degradation and retrograde toxin transport. It is highly expressed in heart and pancreas. Vps11 associates with Vps16, Vps18, and Vps33 to form a Class C Vps core complex that is required for soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE)-mediated membrane fusion at the lysosome-like yeast vacuole. The core complex, together with two additional compartment-specific subunits, forms the tethering complexes HOPS (homotypic vacuole fusion and protein sorting) and CORVET (class C core vacuole/endosome transport). CORVET contains the additional Vps3 and Vps8 subunits. It operates at endosomes, controls traffic into late endosomes and interacts with the Rab5/Vps21-GTP form. HOPS contains the additional Vps39 and Vps41 subunits. It operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form. Vps11 is a central scaffold protein upon which both HOPS and CORVET assemble. The HOPS and CORVET complexes disassemble in the absence of Vps11, resulting in massive fragmentation of vacuoles. Vps11 contains a clathrin repeat domain and a C-terminal C3H2C3-type RING-H2 finger. This subfamily also includes Vps11 homologs found in fungi, such as Saccharomyces cerevisiae vacuolar membrane protein Pep5p, also known as carboxypeptidase Y-deficient protein 5, vacuolar morphogenesis protein 1, or vacuolar biogenesis protein END1. Pep5p is essential for vacuolar biogenesis. It associates with Pep3p to form a core Pep3p/Pep5p complex that promotes vesicular docking/fusion reactions in conjunction with SNARE proteins at multiple steps in transport routes to the vacuole.


Pssm-ID: 438349 [Multi-domain]  Cd Length: 44  Bit Score: 35.79  E-value: 8.58e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2073512899  318 SRCGVCEQLLRDPVIT-TCGHSFCRQCISSYwsqsgPSGDYSCPQCRKR 365
Cdd:cd16688      1 TKCSACGSTLDLPSVHfLCGHSFHQHCLEDY-----EENDRECPLCAPE 44
RING-HC_MuRF3 cd16761
RING finger, HC subclass, found in muscle-specific RING finger protein 3 (MuRF-3) and similar ...
 320-363 9.24e-03

RING finger, HC subclass, found in muscle-specific RING finger protein 3 (MuRF-3) and similar proteins; MuRF-3, also known as tripartite motif-containing protein 54 (TRIM54), or RING finger protein 30 (RNF30), is an E3 ubiquitin-protein ligase in ubiquitin-mediated muscle protein turnover. It is ubiquitously detected in all fibre types, is developmentally upregulated, associates with microtubules, the sarcomeric M-line and Z-line, and is required for microtubule stability and myogenesis. It associates with glutamylated microtubules during skeletal muscle development, and is required for skeletal myoblast differentiation and development of cellular microtubular networks. MuRF-3 controls the degradation of four-and-a-half LIM domain (FHL2) and gamma-filamin and is required for maintenance of ventricular integrity after myocardial infarction (MI). MuRF-3 belongs to the C-II subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, and an acidic residue-rich (AR) domain. It also harbors a MURF family-specific conserved box (MFC) between its RING-HC finger and Bbox domains.


Pssm-ID: 319675 [Multi-domain]  Cd Length: 59  Bit Score: 36.55  E-value: 9.24e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2073512899  320 CGVCEQLLRDPV-ITTCGHSFCRQCISSYWSQSGP------------SGDYSCPQCR 363
Cdd:cd16761      3 CPICLEMFTKPVvILPCQHNLCRKCANDVFQASNPlwqsrgsstvssGGRFRCPSCR 59
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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