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Conserved domains on  [gi|34878777|ref|NP_062538|]
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E3 ubiquitin-protein ligase BRE1A [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RING-HC_RNF20 cd16814
RING finger, HC subclass, found in RING finger protein 20 (RNF20); RNF20, also known as BRE1A ...
902-975 4.25e-50

RING finger, HC subclass, found in RING finger protein 20 (RNF20); RNF20, also known as BRE1A or BRE1, is an E3 ubiquitin-protein ligase that forms a heterodimeric complex together with BRE1B, also known as RNF40, to 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. It regulates the cell cycle and differentiation of neural precursor cells (NPCs), and links histone H2B ubiquitylation with inflammation and inflammation-associated cancer. Moreover, RNF20 promotes the polyubiquitination and proteasome-dependent degradation of transcription factor activator protein 2alpha (AP-2alpha), a negative regulator of adipogenesis by repressing the transcription of CCAAT/enhancer binding protein (C/EBPalpha) gene. Furthermore, RNF20 functions as an additional chromatin regulator that is necessary for mixed-lineage leukemia (MLL)-fusion-mediated leukemogenesis. It also inhibits TFIIS-facilitated transcriptional elongation to suppress pro-oncogenic gene expression. TFIIS is a factor capable of relieving stalled RNA polymerase II. RNF20 contains a C3HC4-type RING-HC finger at its C-terminus.


:

Pssm-ID: 438463 [Multi-domain]  Cd Length: 75  Bit Score: 170.60  E-value: 4.25e-50
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34878777 902 VPKCDEILMEEIKDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIYIG 975
Cdd:cd16814   2 VPNCDEILMEEIKDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIYIG 75
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
322-894 1.96e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 1.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 322 ARKFEEMNAELEENKelAQNRLCELEKLRQDFEEVTTQNEKLKVELRSAVEQVVKETPEYRCMQSQFSVLYNESLQLKAH 401
Cdd:COG1196 212 AERYRELKEELKELE--AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 402 LDEARTLLHGTRGTHQHQVELIERDEVSL------HKKLRTEVIQLEDTLAQVRKEYEMLRIEFEQTLAANEQAGPINRE 475
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLeeleeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 476 MRHLISSLQNHNHQLKGEVLRYKRKLREAQSDLNKTRLRSGSALLQSQSSTEDPKDEPAELKPDSEDLSSQSSASKASQE 555
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 556 DANEIKSKRDEEERERERREKEREREREREKEKEREREKQKLKESEKERDSAKDKEKGkhdDGRKKEAEIIKQLKIELKK 635
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL---EGVKAALLLAGLRGLAGAV 526
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 636 AQESQKEMKLLLDMY-RSAPKEQRDKVQLMAAEKKSKAELEDLRQ-RLKDLEDKEKKENKKMADEDALRKIRAVEEQIEY 713
Cdd:COG1196 527 AVLIGVEAAYEAALEaALAAALQNIVVEDDEVAAAAIEYLKAAKAgRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 714 LQKKLAMAKQEEEALLSEMDVTGQAFEDMQEQNIRLMQQLREkddanfklmsERIKSNQIHKLLKEEKEELADQVLTLKT 793
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE----------VTLEGEGGSAGGSLTGGSRRELLAALLE 676
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 794 QVDAQLQVVRKLEEKEHLLQSNIGTGEKELGLRTQALEMNKRKAMEAAQLADDLKAQLELAQKKLHDFQDEIVENSVTKE 873
Cdd:COG1196 677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL 756
                       570       580
                ....*....|....*....|.
gi 34878777 874 KDMFNFKRAQEDISRLRRKLE 894
Cdd:COG1196 757 PEPPDLEELERELERLEREIE 777
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
177-461 1.33e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    177 RVESSRRAVSQIVTVYDKLQEKVELLSRKLNSgdnliVEEAVQELNSFLAQENMRLQELTDllqEKHRTMSQEFSKLQSK 256
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISE-----LEKRLEEIEQLLEELNKKIKDLGE---EEQLRVKEKIGELEAE 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    257 VETAESRVSVLESMIDDLQwdiDKIRKREQRLNRHLAEVLERvnskgykvygagsslyggtitinARKFEEMNAELEENK 336
Cdd:TIGR02169  303 IASLERSIAEKERELEDAE---ERLAKLEAEIDKLLAEIEEL-----------------------EREIEEERKRRDKLT 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    337 ELAQNRLCELEKLRQDFEEVTTQNEKLKVELRSAVEQVVKETPEYRCMQSQFSVLYNESLQLKAHLDEARTLLHGTRGTH 416
Cdd:TIGR02169  357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 34878777    417 QhqvELIERDEVSLH--KKLRTEVIQLEDTLAQVRKEYEMLRIEFEQ 461
Cdd:TIGR02169  437 N---ELEEEKEDKALeiKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
 
Name Accession Description Interval E-value
RING-HC_RNF20 cd16814
RING finger, HC subclass, found in RING finger protein 20 (RNF20); RNF20, also known as BRE1A ...
902-975 4.25e-50

RING finger, HC subclass, found in RING finger protein 20 (RNF20); RNF20, also known as BRE1A or BRE1, is an E3 ubiquitin-protein ligase that forms a heterodimeric complex together with BRE1B, also known as RNF40, to 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. It regulates the cell cycle and differentiation of neural precursor cells (NPCs), and links histone H2B ubiquitylation with inflammation and inflammation-associated cancer. Moreover, RNF20 promotes the polyubiquitination and proteasome-dependent degradation of transcription factor activator protein 2alpha (AP-2alpha), a negative regulator of adipogenesis by repressing the transcription of CCAAT/enhancer binding protein (C/EBPalpha) gene. Furthermore, RNF20 functions as an additional chromatin regulator that is necessary for mixed-lineage leukemia (MLL)-fusion-mediated leukemogenesis. It also inhibits TFIIS-facilitated transcriptional elongation to suppress pro-oncogenic gene expression. TFIIS is a factor capable of relieving stalled RNA polymerase II. RNF20 contains a C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 438463 [Multi-domain]  Cd Length: 75  Bit Score: 170.60  E-value: 4.25e-50
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34878777 902 VPKCDEILMEEIKDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIYIG 975
Cdd:cd16814   2 VPNCDEILMEEIKDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIYIG 75
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
922-960 4.06e-09

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: 52.90  E-value: 4.06e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 34878777    922 CP-CCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKC 960
Cdd:smart00184   1 CPiCLEEYLKDPVILPCGHTFCRSCIRKWLESGNNTCPIC 40
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
922-960 8.28e-08

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: 49.28  E-value: 8.28e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 34878777   922 CPCCNMRKKDAV-LTKCFHVFCFECVKTRYDTRQRKCPKC 960
Cdd:pfam00097   1 CPICLEEPKDPVtLLPCGHLFCSKCIRSWLESGNVTCPLC 40
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
322-894 1.96e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 1.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 322 ARKFEEMNAELEENKelAQNRLCELEKLRQDFEEVTTQNEKLKVELRSAVEQVVKETPEYRCMQSQFSVLYNESLQLKAH 401
Cdd:COG1196 212 AERYRELKEELKELE--AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 402 LDEARTLLHGTRGTHQHQVELIERDEVSL------HKKLRTEVIQLEDTLAQVRKEYEMLRIEFEQTLAANEQAGPINRE 475
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLeeleeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 476 MRHLISSLQNHNHQLKGEVLRYKRKLREAQSDLNKTRLRSGSALLQSQSSTEDPKDEPAELKPDSEDLSSQSSASKASQE 555
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 556 DANEIKSKRDEEERERERREKEREREREREKEKEREREKQKLKESEKERDSAKDKEKGkhdDGRKKEAEIIKQLKIELKK 635
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL---EGVKAALLLAGLRGLAGAV 526
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 636 AQESQKEMKLLLDMY-RSAPKEQRDKVQLMAAEKKSKAELEDLRQ-RLKDLEDKEKKENKKMADEDALRKIRAVEEQIEY 713
Cdd:COG1196 527 AVLIGVEAAYEAALEaALAAALQNIVVEDDEVAAAAIEYLKAAKAgRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 714 LQKKLAMAKQEEEALLSEMDVTGQAFEDMQEQNIRLMQQLREkddanfklmsERIKSNQIHKLLKEEKEELADQVLTLKT 793
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE----------VTLEGEGGSAGGSLTGGSRRELLAALLE 676
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 794 QVDAQLQVVRKLEEKEHLLQSNIGTGEKELGLRTQALEMNKRKAMEAAQLADDLKAQLELAQKKLHDFQDEIVENSVTKE 873
Cdd:COG1196 677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL 756
                       570       580
                ....*....|....*....|.
gi 34878777 874 KDMFNFKRAQEDISRLRRKLE 894
Cdd:COG1196 757 PEPPDLEELERELERLEREIE 777
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
44-759 1.17e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777     44 EELDIRTLQTKNRKLAEMLDQRQAIEDELREHIEKLERRQATDDASLLIVNRYWSQFDENIRIILKRYDLEQGLGDLLTE 123
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    124 RKALVVPEPEPDSDSNQERKDDRERGEGQEPAFSFLATLASSSSEEMESQ---LQERVESSRRAVSQIVTVYDKLQEKVE 200
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEElesLEAELEELEAELEELESRLEELEEQLE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    201 LLSRKLNSgdnliVEEAVQELNSFLAQENMRLQELTDLLQEKHRTMSQEFSKLQS-KVETAESRVSVLESMIDDLQWDID 279
Cdd:TIGR02168  383 TLRSKVAQ-----LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELE 457
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    280 KIRKREQRLNRHLAEVLERVNSKGYKVYGAGSSLyggtitinarkfeEMNAELEENKELAQNRLCELEKLRQDFEEVTTQ 359
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALDAAERELAQLQARL-------------DSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    360 -NEKLKVE--LRSAVEQVVKETPEYRCMQSQFSVLYNESLqLKAHLDEARTLLHGTRGTHQH------QVELIERDEVSL 430
Cdd:TIGR02168  525 lSELISVDegYEAAIEAALGGRLQAVVVENLNAAKKAIAF-LKQNELGRVTFLPLDSIKGTEiqgndrEILKNIEGFLGV 603
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    431 HKKLRTEVIQLEDTLaqvrkEYEMLRIEFEQTLA-ANEQAGPINREMRhlISSLQnhNHQLKGEVLRYKRKLREAQSDLN 509
Cdd:TIGR02168  604 AKDLVKFDPKLRKAL-----SYLLGGVLVVDDLDnALELAKKLRPGYR--IVTLD--GDLVRPGGVITGGSAKTNSSILE 674
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    510 KTR--LRSGSALLQSQSSTEDPKDEPAELKPDSEDLSSQSSASKASQEDAnEIKSKRDEEERERERREKEREREREREKE 587
Cdd:TIGR02168  675 RRReiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERIAQLS 753
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    588 KEREREKQKLKESEKERDSAKDKEKgKHDDGRKKEAEIIKQLKIELKKAQESQKEMKLLLDMYRSAPKEQRDKVQLMAAE 667
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    668 KKSKA-ELEDLRQRLKDLEDKEKKENKKMADEDALrkIRAVEEQIEYLQKKLAMAKQEEEALLSEMDVTGQAFEDMQEQN 746
Cdd:TIGR02168  833 IAATErRLEDLEEQIEELSEDIESLAAEIEELEEL--IEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
                          730
                   ....*....|...
gi 34878777    747 IRLMQQLREKDDA 759
Cdd:TIGR02168  911 SELRRELEELREK 923
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
187-896 8.40e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 50.12  E-value: 8.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    187 QIVTVYDKLQEKVELLSRKLNSGDNL------IVEEAVQELNSFLAQENMRLQELTDLLQEKHRTMSQEFSKLQSKVETA 260
Cdd:pfam15921   75 HIERVLEEYSHQVKDLQRRLNESNELhekqkfYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHEL 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    261 ESRVSVLESMIDDLQWDIDKIRK----REQRLNRHLAEVLERVNSKGYKVYGAGS------SLYGGTITINARKFEE--- 327
Cdd:pfam15921  155 EAAKCLKEDMLEDSNTQIEQLRKmmlsHEGVLQEIRSILVDFEEASGKKIYEHDSmstmhfRSLGSAISKILRELDTeis 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    328 --------MNAELEENKELAQNRLCELEKLRQD-FEEVTTQNEklkVELRSAVEQVVKETPEYRCMQSQFSVLYNESL-- 396
Cdd:pfam15921  235 ylkgrifpVEDQLEALKSESQNKIELLLQQHQDrIEQLISEHE---VEITGLTEKASSARSQANSIQSQLEIIQEQARnq 311
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    397 ---------QLKAHLDEARTLLHGTRGTHQHQVELIERDEVSLHKKL---RTEV-----------IQLEDTLAQVRKEYE 453
Cdd:pfam15921  312 nsmymrqlsDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELteaRTERdqfsqesgnldDQLQKLLADLHKREK 391
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    454 MLRIEFEQTLAANEQAGPINREMRHLISSLQNHNHqlkgEVLRYKRKLREAQSDLNKTRLRSGSALLQSQSSTEDPKDEP 533
Cdd:pfam15921  392 ELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM----EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLT 467
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    534 AELKPDSEDLssqssasKASQEDANEIKSKRDEEERERERREKEREREREREKEKEREREKQKLKESEKERDSAKDKEKG 613
Cdd:pfam15921  468 AQLESTKEML-------RKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEG 540
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    614 KHDDGRKKEAEIIKQLKIELKKA-----QESQKEMKLLLDMYRSAPKEQRDKVQLMAAEKKSKAELEDLRQrLKDLEDKE 688
Cdd:pfam15921  541 DHLRNVQTECEALKLQMAEKDKVieilrQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKI-LKDKKDAK 619
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    689 KKENKKMADEDALRKIRAVEEQIEYLqKKLAMAKQEEEALLSEMDVTGQAFEDMQEQNIRLMQQLREKDD-----ANFKL 763
Cdd:pfam15921  620 IRELEARVSDLELEKVKLVNAGSERL-RAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEemettTNKLK 698
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    764 MSERIKSNQIHKLLKEEKEELADQVLTLKTQVDAQLQVVRK------LEEKEHLLQSNIGTGEKELGLRTQALEMNKRKA 837
Cdd:pfam15921  699 MQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKrgqidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQEL 778
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34878777    838 MEAAQLADDLKAQLELAQKKLHDFQDEIVENSVTKEKDMFNFKRAQEDISR-----LRRKLETT 896
Cdd:pfam15921  779 STVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRqeqesVRLKLQHT 842
PTZ00121 PTZ00121
MAEBL; Provisional
498-898 3.24e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777   498 KRKLREAQSDLNKTRLRSGSALLQSQSSTEDPKDEPAELKPDSEDLSSQSSASKASQEDANEIKSKRDEEERERERREKE 577
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777   578 REREREREKEKEREREKQKLKESEKERDSAKDKEKGKHDDGRKKEAEIIKQLKIELKKAQESQK--EMKLLLDMYRSAPK 655
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKkaEEAKKADEAKKKAE 1480
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777   656 EQRDKVQLMAAEKKSKAELEDLRQRlkdledkekKENKKMADEdalrkIRAVEEqieylQKKLAMAKQEEEAllSEMDVT 735
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKA---------AEAKKKADE-----AKKAEE-----AKKADEAKKAEEA--KKADEA 1539
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777   736 GQAFEDMQEQNIRLMQQLREkddanfklmSERIKSNQIHKLLKEEKEELADQVLTLKTQVDAQLQVVRKLEEKEHLLQSN 815
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKK---------AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777   816 IGTGEKELGLRTQALemnkRKAMEAAQLADDLKAQLELAQKKLHDFQDEIVENSVTKEKDMfnfKRAQEDisrlRRKLET 895
Cdd:PTZ00121 1611 EAKKAEEAKIKAEEL----KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA---KKAEED----KKKAEE 1679

                  ...
gi 34878777   896 TKK 898
Cdd:PTZ00121 1680 AKK 1682
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
177-461 1.33e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    177 RVESSRRAVSQIVTVYDKLQEKVELLSRKLNSgdnliVEEAVQELNSFLAQENMRLQELTDllqEKHRTMSQEFSKLQSK 256
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISE-----LEKRLEEIEQLLEELNKKIKDLGE---EEQLRVKEKIGELEAE 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    257 VETAESRVSVLESMIDDLQwdiDKIRKREQRLNRHLAEVLERvnskgykvygagsslyggtitinARKFEEMNAELEENK 336
Cdd:TIGR02169  303 IASLERSIAEKERELEDAE---ERLAKLEAEIDKLLAEIEEL-----------------------EREIEEERKRRDKLT 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    337 ELAQNRLCELEKLRQDFEEVTTQNEKLKVELRSAVEQVVKETPEYRCMQSQFSVLYNESLQLKAHLDEARTLLHGTRGTH 416
Cdd:TIGR02169  357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 34878777    417 QhqvELIERDEVSLH--KKLRTEVIQLEDTLAQVRKEYEMLRIEFEQ 461
Cdd:TIGR02169  437 N---ELEEEKEDKALeiKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
215-382 3.02e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 3.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 215 EEAVQELNSfLAQENMRLQELTDLLQEKHRTMSQEFSKLQSKVETAESRVSVLESMIDDLQWDIDKIRKREQRLNRHLAE 294
Cdd:COG4942  23 AEAEAELEQ-LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 295 VLERVNSKGYKVYGAGS--------------------SLYGGTITINARKFEEMNA---ELEENKELAQNRLCELEKLRQ 351
Cdd:COG4942 102 QKEELAELLRALYRLGRqpplalllspedfldavrrlQYLKYLAPARREQAEELRAdlaELAALRAELEAERAELEALLA 181
                       170       180       190
                ....*....|....*....|....*....|.
gi 34878777 352 DFEEVTTQNEKLKVELRSAVEQVVKETPEYR 382
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELA 212
46 PHA02562
endonuclease subunit; Provisional
174-378 4.43e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777  174 LQERVESSRRAVSQIVTVYDKLQEKVELLSRKLNSgdnliVEEAVQELNSFLAQENMRLQELTDLLQ--EKHR---TMSQ 248
Cdd:PHA02562 218 KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIED-----PSAALNKLNTAAAKIKSKIEQFQKVIKmyEKGGvcpTCTQ 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777  249 EFSKLQSKVETAESRVSVLESMIDDLQWDIDKIRKREQRLNRHLAEVLErVNSKgykvygagSSLYGGTITINARKFEEM 328
Cdd:PHA02562 293 QISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE-LKNK--------ISTNKQSLITLVDKAKKV 363
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 34878777  329 NAELEENKELAQNRLCELEKLRQDFEEVTTQNEKLKVEL--RSAVEQVVKET 378
Cdd:PHA02562 364 KAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKyhRGIVTDLLKDS 415
 
Name Accession Description Interval E-value
RING-HC_RNF20 cd16814
RING finger, HC subclass, found in RING finger protein 20 (RNF20); RNF20, also known as BRE1A ...
902-975 4.25e-50

RING finger, HC subclass, found in RING finger protein 20 (RNF20); RNF20, also known as BRE1A or BRE1, is an E3 ubiquitin-protein ligase that forms a heterodimeric complex together with BRE1B, also known as RNF40, to 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. It regulates the cell cycle and differentiation of neural precursor cells (NPCs), and links histone H2B ubiquitylation with inflammation and inflammation-associated cancer. Moreover, RNF20 promotes the polyubiquitination and proteasome-dependent degradation of transcription factor activator protein 2alpha (AP-2alpha), a negative regulator of adipogenesis by repressing the transcription of CCAAT/enhancer binding protein (C/EBPalpha) gene. Furthermore, RNF20 functions as an additional chromatin regulator that is necessary for mixed-lineage leukemia (MLL)-fusion-mediated leukemogenesis. It also inhibits TFIIS-facilitated transcriptional elongation to suppress pro-oncogenic gene expression. TFIIS is a factor capable of relieving stalled RNA polymerase II. RNF20 contains a C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 438463 [Multi-domain]  Cd Length: 75  Bit Score: 170.60  E-value: 4.25e-50
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34878777 902 VPKCDEILMEEIKDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIYIG 975
Cdd:cd16814   2 VPNCDEILMEEIKDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIYIG 75
RING-HC_RNF20-like cd16704
RING finger, HC subclass, found in RING finger protein RNF20, RNF40, and similar proteins; ...
910-974 4.75e-44

RING finger, HC subclass, found in RING finger protein RNF20, RNF40, and similar proteins; RNF20, also known as BRE1A, and RNF40, also known as BRE1B, are E3 ubiquitin-protein ligases that work together to form a heterodimeric 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. RNF20 regulates the cell cycle and differentiation of neural precursor cells (NPCs) and links histone H2B ubiquitylation with inflammation and inflammation-associated cancer. RNF40, also known as 95 kDa retinoblastoma-associated protein (RBP95), was identified as a novel leucine zipper retinoblastoma protein (pRb)-associated protein that may function as a regulation factor in RNA polymerase II-mediated transcription and/or transcriptional processing. All subfamily members contain a C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 438364 [Multi-domain]  Cd Length: 65  Bit Score: 152.99  E-value: 4.75e-44
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34878777 910 MEEIKDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIYI 974
Cdd:cd16704   1 LEEIKEYKARLTCPCCNTRKKDAVLTKCFHVFCFECLKTRYETRQRKCPKCNAAFGANDFHRIYI 65
RING-HC_RNF40 cd16815
RING finger, HC subclass, found in RING finger protein 40 (RNF40); RNF40, also known as BRE1B ...
897-974 7.15e-41

RING finger, HC subclass, found in RING finger protein 40 (RNF40); RNF40, also known as BRE1B or 95 kDa retinoblastoma-associated protein (RBP95), was identified as a novel leucine zipper retinoblastoma protein (pRb)-associated protein that may function as a regulation factor in RNA polymerase II-mediated transcription and/or transcriptional processing. RNF40 also functions as an E3 ubiquitin-protein ligase that forms a heterodimeric complex with BRE1B, also known as RNF40, to 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. It cooperates with SUPT16H to induce dynamic changes in chromatin structure during DSB repair. RNF40 contains a C3HC4-type RING-HC finger at the C-terminus.


Pssm-ID: 438464 [Multi-domain]  Cd Length: 78  Bit Score: 144.40  E-value: 7.15e-41
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34878777 897 KKPDNVPKCDEILMEEIKDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIYI 974
Cdd:cd16815   1 KKVEVYADADEILQEEIKEYKARLTCPCCNTRKKDAVLTKCFHVFCFECVKTRYESRQRKCPKCNAAFGAHDFHRIYI 78
RING-HC_dBre1-like cd16705
RING finger, HC subclass, found in Drosophila melanogaster Bre1 (dBre1) and similar proteins; ...
906-974 2.58e-37

RING finger, HC subclass, found in Drosophila melanogaster Bre1 (dBre1) and similar proteins; dBre1 is the functional homolog of yeast Bre1, an E3 ubiquitin ligase required for the monoubiquitination of histone H2B and, indirectly, for H3K4 methylation. dBre1 acts as a nuclear component required for the expression of Notch target genes in Drosophila development. dBre1 contains a C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 438365 [Multi-domain]  Cd Length: 69  Bit Score: 133.93  E-value: 2.58e-37
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34878777 906 DEILMEEIKDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIYI 974
Cdd:cd16705   1 DEVLMEEIREYKEQLTCPSCKVKRKDAVLTKCFHVFCLDCLRTRYETRQRKCPKCNAAFGANDYHRLYL 69
RING-HC_Bre1-like cd16499
RING finger, HC subclass, found in yeast Bre1 and its homologs from eukaryotes; Bre1 is an E3 ...
914-972 4.55e-31

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: 115.73  E-value: 4.55e-31
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 34878777 914 KDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRI 972
Cdd:cd16499   1 KDLRELLKCSVCNDRFKDVIITKCGHVFCNECVQKRLETRQRKCPGCGKAFGANDVQRI 59
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
920-960 5.48e-11

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: 58.27  E-value: 5.48e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 34878777 920 LTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKC 960
Cdd:cd16449   1 LECPICLERLKDPVLLPCGHVFCRECIRRLLESGSIKCPIC 41
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
922-960 4.06e-09

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: 52.90  E-value: 4.06e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 34878777    922 CP-CCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKC 960
Cdd:smart00184   1 CPiCLEEYLKDPVILPCGHTFCRSCIRKWLESGNNTCPIC 40
RING-HC_COP1 cd16504
RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and ...
920-961 8.99e-09

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: 52.24  E-value: 8.99e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 34878777 920 LTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRkCPKCN 961
Cdd:cd16504   3 FLCPICFDIIKEAFVTKCGHSFCYKCIVKHLEQKNR-CPKCN 43
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
922-960 8.28e-08

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: 49.28  E-value: 8.28e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 34878777   922 CPCCNMRKKDAV-LTKCFHVFCFECVKTRYDTRQRKCPKC 960
Cdd:pfam00097   1 CPICLEEPKDPVtLLPCGHLFCSKCIRSWLESGNVTCPLC 40
RING-HC_CHR27-like cd23142
RING finger, HC subclass, found in Arabidopsis thaliana protein CHROMATIN REMODELING 27 (CHR27) ...
922-968 1.03e-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: 49.49  E-value: 1.03e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 34878777 922 CPCCNMRKKDAVLTKCFHVFCFECVKTRY----DTRQR-KCPKCNAAFGAND 968
Cdd:cd23142   3 CPICNDPPEDAVVTLCGHVFCCECVFQYLssdrTCRQFnHCPLCRQKLYLDD 54
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
322-894 1.96e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 1.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 322 ARKFEEMNAELEENKelAQNRLCELEKLRQDFEEVTTQNEKLKVELRSAVEQVVKETPEYRCMQSQFSVLYNESLQLKAH 401
Cdd:COG1196 212 AERYRELKEELKELE--AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 402 LDEARTLLHGTRGTHQHQVELIERDEVSL------HKKLRTEVIQLEDTLAQVRKEYEMLRIEFEQTLAANEQAGPINRE 475
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLeeleeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 476 MRHLISSLQNHNHQLKGEVLRYKRKLREAQSDLNKTRLRSGSALLQSQSSTEDPKDEPAELKPDSEDLSSQSSASKASQE 555
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 556 DANEIKSKRDEEERERERREKEREREREREKEKEREREKQKLKESEKERDSAKDKEKGkhdDGRKKEAEIIKQLKIELKK 635
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL---EGVKAALLLAGLRGLAGAV 526
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 636 AQESQKEMKLLLDMY-RSAPKEQRDKVQLMAAEKKSKAELEDLRQ-RLKDLEDKEKKENKKMADEDALRKIRAVEEQIEY 713
Cdd:COG1196 527 AVLIGVEAAYEAALEaALAAALQNIVVEDDEVAAAAIEYLKAAKAgRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 714 LQKKLAMAKQEEEALLSEMDVTGQAFEDMQEQNIRLMQQLREkddanfklmsERIKSNQIHKLLKEEKEELADQVLTLKT 793
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE----------VTLEGEGGSAGGSLTGGSRRELLAALLE 676
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 794 QVDAQLQVVRKLEEKEHLLQSNIGTGEKELGLRTQALEMNKRKAMEAAQLADDLKAQLELAQKKLHDFQDEIVENSVTKE 873
Cdd:COG1196 677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL 756
                       570       580
                ....*....|....*....|.
gi 34878777 874 KDMFNFKRAQEDISRLRRKLE 894
Cdd:COG1196 757 PEPPDLEELERELERLEREIE 777
RING-HC_RNF138 cd16544
RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; ...
918-961 3.17e-07

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: 47.78  E-value: 3.17e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 34878777 918 ARLTCPCCNMRKKDAV-LTKCFHVFCFECVKTRYDTRQRKCPKCN 961
Cdd:cd16544   1 AELTCPVCQEVLKDPVeLPPCRHIFCKACILLALRSSGARCPLCR 45
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
620-897 3.30e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 3.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 620 KKEAEIIKQ----LKIELKKAQESQKEMKLLldmyrsapKEQRDKVQLMAAEKKSKAELEDLRQRLKDLEDKEKKENKkm 695
Cdd:COG1196 219 KEELKELEAelllLKLRELEAELEELEAELE--------ELEAELEELEAELAELEAELEELRLELEELELELEEAQA-- 288
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 696 ADEDALRKIRAVEEQIEYLQKKLAMAKQEEEALLSEMDVTGQAFEDMQEQNIRLMQQLREKDDANFKLMSERIKSNQIHK 775
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 776 LLKEEKEELADQVLTLKTQVDAQLQVVRKLEEKEHLLQSNIGTGEKELGLRTQALEMNKRKAMEAAQLADDLKAQLELAQ 855
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 34878777 856 KKLHDFQDEIVENSVTKEKDMFNFKRAQEDISRLRRKLETTK 897
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
44-759 1.17e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777     44 EELDIRTLQTKNRKLAEMLDQRQAIEDELREHIEKLERRQATDDASLLIVNRYWSQFDENIRIILKRYDLEQGLGDLLTE 123
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    124 RKALVVPEPEPDSDSNQERKDDRERGEGQEPAFSFLATLASSSSEEMESQ---LQERVESSRRAVSQIVTVYDKLQEKVE 200
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEElesLEAELEELEAELEELESRLEELEEQLE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    201 LLSRKLNSgdnliVEEAVQELNSFLAQENMRLQELTDLLQEKHRTMSQEFSKLQS-KVETAESRVSVLESMIDDLQWDID 279
Cdd:TIGR02168  383 TLRSKVAQ-----LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELE 457
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    280 KIRKREQRLNRHLAEVLERVNSKGYKVYGAGSSLyggtitinarkfeEMNAELEENKELAQNRLCELEKLRQDFEEVTTQ 359
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALDAAERELAQLQARL-------------DSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    360 -NEKLKVE--LRSAVEQVVKETPEYRCMQSQFSVLYNESLqLKAHLDEARTLLHGTRGTHQH------QVELIERDEVSL 430
Cdd:TIGR02168  525 lSELISVDegYEAAIEAALGGRLQAVVVENLNAAKKAIAF-LKQNELGRVTFLPLDSIKGTEiqgndrEILKNIEGFLGV 603
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    431 HKKLRTEVIQLEDTLaqvrkEYEMLRIEFEQTLA-ANEQAGPINREMRhlISSLQnhNHQLKGEVLRYKRKLREAQSDLN 509
Cdd:TIGR02168  604 AKDLVKFDPKLRKAL-----SYLLGGVLVVDDLDnALELAKKLRPGYR--IVTLD--GDLVRPGGVITGGSAKTNSSILE 674
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    510 KTR--LRSGSALLQSQSSTEDPKDEPAELKPDSEDLSSQSSASKASQEDAnEIKSKRDEEERERERREKEREREREREKE 587
Cdd:TIGR02168  675 RRReiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERIAQLS 753
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    588 KEREREKQKLKESEKERDSAKDKEKgKHDDGRKKEAEIIKQLKIELKKAQESQKEMKLLLDMYRSAPKEQRDKVQLMAAE 667
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    668 KKSKA-ELEDLRQRLKDLEDKEKKENKKMADEDALrkIRAVEEQIEYLQKKLAMAKQEEEALLSEMDVTGQAFEDMQEQN 746
Cdd:TIGR02168  833 IAATErRLEDLEEQIEELSEDIESLAAEIEELEEL--IEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
                          730
                   ....*....|...
gi 34878777    747 IRLMQQLREKDDA 759
Cdd:TIGR02168  911 SELRRELEELREK 923
RING-HC_Topors cd16574
RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein ...
921-964 1.67e-06

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: 45.74  E-value: 1.67e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 34878777 921 TCPCC--NMRKKDAVLTKCFHVFCFECVKtRYDTRQRKCPKCNAAF 964
Cdd:cd16574   3 SCPICldRFENEKAFLDGCFHAFCFTCIL-EWSKVKNECPLCKQPF 47
RING-HC_RNF10 cd16536
RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 ...
921-968 2.09e-06

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


Pssm-ID: 438198 [Multi-domain]  Cd Length: 54  Bit Score: 45.69  E-value: 2.09e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 34878777 921 TCPCCNMRKKDAVLTKCFHVFCFECVKtRY----DTRQRKCPKCNAAFGAND 968
Cdd:cd16536   2 QCPICLEPPVAPRITRCGHIFCWPCIL-RYlslsEKKWRKCPICFESIHKKD 52
RING-HC_RNFT1-like cd16532
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein ...
921-960 6.07e-06

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: 43.83  E-value: 6.07e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 34878777 921 TCPCCNMRKKDAVLTKCFHVFCFECVKTRYDtRQRKCPKC 960
Cdd:cd16532   2 ICPICQDEFKDPVVLRCKHIFCEDCVSEWFE-RERTCPLC 40
RING-HC_RNF39 cd16592
RING finger, HC subclass, found in RING finger protein 39 (RNF39) and similar proteins; RNF39, ...
921-964 7.02e-06

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: 44.36  E-value: 7.02e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 34878777 921 TCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRK--------CPKCNAAF 964
Cdd:cd16592   6 TCPICLGYFKDPVILDCEHSFCRACIARHWGQEAMEgngaegvfCPQCGEPC 57
RING-HC_TRIM77_C-IV cd16543
RING finger, HC subclass, found in tripartite motif-containing protein 77 (TRIM77) and similar ...
918-964 8.20e-06

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: 43.92  E-value: 8.20e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 34878777 918 ARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQ--RKCPKCNAAF 964
Cdd:cd16543   2 DQLTCSICLDLLKDPVTIPCGHSFCMNCITLLWDRKQgvPSCPQCRESF 50
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
187-896 8.40e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 50.12  E-value: 8.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    187 QIVTVYDKLQEKVELLSRKLNSGDNL------IVEEAVQELNSFLAQENMRLQELTDLLQEKHRTMSQEFSKLQSKVETA 260
Cdd:pfam15921   75 HIERVLEEYSHQVKDLQRRLNESNELhekqkfYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHEL 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    261 ESRVSVLESMIDDLQWDIDKIRK----REQRLNRHLAEVLERVNSKGYKVYGAGS------SLYGGTITINARKFEE--- 327
Cdd:pfam15921  155 EAAKCLKEDMLEDSNTQIEQLRKmmlsHEGVLQEIRSILVDFEEASGKKIYEHDSmstmhfRSLGSAISKILRELDTeis 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    328 --------MNAELEENKELAQNRLCELEKLRQD-FEEVTTQNEklkVELRSAVEQVVKETPEYRCMQSQFSVLYNESL-- 396
Cdd:pfam15921  235 ylkgrifpVEDQLEALKSESQNKIELLLQQHQDrIEQLISEHE---VEITGLTEKASSARSQANSIQSQLEIIQEQARnq 311
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    397 ---------QLKAHLDEARTLLHGTRGTHQHQVELIERDEVSLHKKL---RTEV-----------IQLEDTLAQVRKEYE 453
Cdd:pfam15921  312 nsmymrqlsDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELteaRTERdqfsqesgnldDQLQKLLADLHKREK 391
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    454 MLRIEFEQTLAANEQAGPINREMRHLISSLQNHNHqlkgEVLRYKRKLREAQSDLNKTRLRSGSALLQSQSSTEDPKDEP 533
Cdd:pfam15921  392 ELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM----EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLT 467
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    534 AELKPDSEDLssqssasKASQEDANEIKSKRDEEERERERREKEREREREREKEKEREREKQKLKESEKERDSAKDKEKG 613
Cdd:pfam15921  468 AQLESTKEML-------RKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEG 540
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    614 KHDDGRKKEAEIIKQLKIELKKA-----QESQKEMKLLLDMYRSAPKEQRDKVQLMAAEKKSKAELEDLRQrLKDLEDKE 688
Cdd:pfam15921  541 DHLRNVQTECEALKLQMAEKDKVieilrQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKI-LKDKKDAK 619
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    689 KKENKKMADEDALRKIRAVEEQIEYLqKKLAMAKQEEEALLSEMDVTGQAFEDMQEQNIRLMQQLREKDD-----ANFKL 763
Cdd:pfam15921  620 IRELEARVSDLELEKVKLVNAGSERL-RAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEemettTNKLK 698
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    764 MSERIKSNQIHKLLKEEKEELADQVLTLKTQVDAQLQVVRK------LEEKEHLLQSNIGTGEKELGLRTQALEMNKRKA 837
Cdd:pfam15921  699 MQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKrgqidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQEL 778
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 34878777    838 MEAAQLADDLKAQLELAQKKLHDFQDEIVENSVTKEKDMFNFKRAQEDISR-----LRRKLETT 896
Cdd:pfam15921  779 STVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRqeqesVRLKLQHT 842
RING-HC_HLTF cd16509
RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar ...
922-968 9.18e-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: 43.83  E-value: 9.18e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 34878777 922 CPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGAND 968
Cdd:cd16509   6 CAICLDSLTNPVITPCAHVFCRRCICEVIQREKAKCPMCRAPLSASD 52
vRING-HC-C4C4_RBBP6 cd16620
Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) ...
920-969 9.37e-06

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: 43.93  E-value: 9.37e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 34878777 920 LTCPCCNMRKKDAVLTK-CFHVFCFECVKTRYDTRQRKCPKCNAAFGANDF 969
Cdd:cd16620   4 LKCPICKDLMKDAVLTPcCGNSFCDECIRTALLEEDFTCPTCKEPDVSPDA 54
RING-HC_RNF185 cd16744
RING finger, HC subclass, found in RING finger protein 185 (RNF185) and similar proteins; ...
922-973 2.00e-05

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: 42.99  E-value: 2.00e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 34878777 922 CPCCNMRKKDAVLTKCFHVFCFECVKTRYDTR--QRKCPKCNAAFGANDFHRIY 973
Cdd:cd16744   3 CNICLDTAKDAVVSLCGHLFCWPCLHQWLETRpnRQVCPVCKAGISRDKVIPLY 56
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
56-719 3.84e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 3.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777  56 RKLAEM---LDQRQAIEDELREHIEKLER--RQAtddasllivNRYwsqfdENIRIILKRYDLEQglgdLLTERKALvvp 130
Cdd:COG1196 179 RKLEATeenLERLEDILGELERQLEPLERqaEKA---------ERY-----RELKEELKELEAEL----LLLKLREL--- 237
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 131 epepdsdSNQERKDDRERGEGQEpafsflatlASSSSEEMESQLQERVESSRRAVSQIVTVYDKLQEKVELLSRKLnsgd 210
Cdd:COG1196 238 -------EAELEELEAELEELEA---------ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL---- 297
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 211 nlivEEAVQELNSfLAQENMRLQELTDLLQEKHRTMSQEFSKLQSKVETAESRVSVLESMIDDLQWDIDKIRKREQRLNR 290
Cdd:COG1196 298 ----ARLEQDIAR-LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 291 HLAEVLERVNSKgykvygagsslyggtitiNARKFEEMNAELEENKELAQNRLcELEKLRQDFEEVTTQNEKLKVELRSA 370
Cdd:COG1196 373 ELAEAEEELEEL------------------AEELLEALRAAAELAAQLEELEE-AEEALLERLERLEEELEELEEALAEL 433
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 371 VEQVVKETPEYRCMQSQFSVLYNESLQLKAHLDEARTLLHGTRgtHQHQVELIERDEVSLHKKLRTEVIQLEDTLAQVRK 450
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE--AALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 451 EYEMLRIEFEQTLAANEQAGPINREMRHLISSLQNHNHQLKGEVLRYKRKLREAQSDLNKTRLRSGSALLQSQSSTEDPK 530
Cdd:COG1196 512 AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAA 591
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 531 DEPAELKPDSEDLSSQSSASKASQEDANEIKSKRDEEERERERREKEREREREREKEKEREREKQKLKESEKERdsaKDK 610
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG---SRR 668
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 611 EKGKHDDGRKKEAEIIKQLKIELKKAQESQKEMKLLLDMYRSAPKEQRDKVQLMAAEKKSKAELEDLRQRLKDLEDKEKK 690
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
                       650       660
                ....*....|....*....|....*....
gi 34878777 691 ENKKMADEDALRKIRAVEEQIEYLQKKLA 719
Cdd:COG1196 749 EEEALEELPEPPDLEELERELERLEREIE 777
RING-HC_RNFT2 cd16742
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2 ...
922-963 4.77e-05

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: 42.17  E-value: 4.77e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 34878777 922 CPCCNMRKKDAVLTKCFHVFCFECVKTRYDtRQRKCPKCNAA 963
Cdd:cd16742  16 CAICQAEFREPLILICQHVFCEECLCLWFD-RERTCPLCRSV 56
mRING-HC-C4C4_TRIM37_C-VIII cd16619
Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 ...
920-960 5.10e-05

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: 41.19  E-value: 5.10e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 34878777 920 LTCPCCNMRKKDAVL-TKCFHVFCFECVKTRYDTRQRKCPKC 960
Cdd:cd16619   1 FRCFICMEKLRDPRLcPHCSKLFCKGCIRRWLSEQRSSCPHC 42
RING-HC_TRIM69_C-IV cd16611
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar ...
909-968 7.39e-05

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: 41.28  E-value: 7.39e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34878777 909 LMEEikdykarLTCPCCNMRKKDAVLTKCFHVFCFECVkTRYDTRQRK---CPKCNAAFGAND 968
Cdd:cd16611   1 LTEE-------LHCPLCLDFFRDPVMLSCGHNFCQSCI-TGFWELQAEdttCPECRELCQYRN 55
RING-HC_NHL-1-like cd16524
RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and ...
920-962 9.11e-05

RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and similar proteins; NHL-1 functions as an E3 ubiquitin-protein ligase in the presence of both UBC-13 and UBC-1 within the ubiquitin pathway of Caenorhabditis elegans. It acts in chemosensory neurons to promote stress resistance in distal tissues by the transcription factor DAF-16 activation but is dispensable for the activation of heat shock factor 1 (HSF-1). NHL-1 belongs to the TRIM (tripartite motif)-NHL 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 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: 438187 [Multi-domain]  Cd Length: 53  Bit Score: 40.87  E-value: 9.11e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 34878777 920 LTCPCCNMRKKDAVLTKCFHVFCFE-CVKTRYD--TRQRKCPKCNA 962
Cdd:cd16524   6 LTCPICLDRYRRPKLLPCQHTFCLSpCLEGLVDyvTRKLKCPECRA 51
RING-HC_TRIM7-like_C-IV cd16594
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM7, TRIM11 and ...
920-969 9.90e-05

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: 41.13  E-value: 9.90e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 34878777 920 LTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRK--CPKCNAAFGANDF 969
Cdd:cd16594   6 LTCPICLDYFTDPVTLDCGHSFCRACIARCWEEPETSasCPQCRETCPQRNL 57
zf-RING_5 pfam14634
zinc-RING finger domain;
922-961 1.20e-04

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 40.49  E-value: 1.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 34878777   922 CP-CCNMRKKD--AVLTKCFHVFCFECVKTryDTRQRKCPKCN 961
Cdd:pfam14634   2 CNkCFKELSKTrpFYLTSCGHIFCEECLTR--LLQERQCPICK 42
RING-HC_RNF207 cd16558
RING finger, HC subclass, found in RING finger protein 207 (RNF207) and similar proteins; ...
920-960 1.22e-04

RING finger, HC subclass, found in RING finger protein 207 (RNF207) and similar proteins; RNF207 is a cardiac-specific E3 ubiquitin-protein ligase that plays an important role in the regulation of cardiac repolarization. It regulates action potential duration, likely via effects on human ether-a-go-go-related gene (HERG) trafficking and localization in a heat shock protein-dependent manner. RNF207 contains a C3HC4-type RING-HC finger, Bbox 1 and Bbox C-terminal (BBC) domain, as well as a C-terminal non-homologous region (CNHR).


Pssm-ID: 438220 [Multi-domain]  Cd Length: 43  Bit Score: 40.42  E-value: 1.22e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 34878777 920 LTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKC 960
Cdd:cd16558   2 LVCYLCHEQYEHPCLLDCYHTFCASCLRGRAADGRLTCPLC 42
RING-HC_PCGF6 cd16738
RING finger found in polycomb group RING finger protein 6 (PCGF6) and similar proteins; PCGF6, ...
913-961 1.27e-04

RING finger found in polycomb group RING finger protein 6 (PCGF6) and similar proteins; PCGF6, also known as Mel18 and Bmi1-like RING finger (MBLR), or RING finger protein 134 (RNF134), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR). It serves as the core component of a noncanonical Polycomb repressive complex 1 (PRC1)-like L3MBTL2 complex, which is composed of some canonical components, such as RNF2, CBX3, CXB4, CXB6, CXB7, and CXB8, as well as some noncanonical components, such as L3MBTL2, E2F6, WDR5, HDAC1, and RYBP, and plays a critical role in epigenetic transcriptional silencing in higher eukaryotes. Like other PCGF homologs, PCGF6 possesses the transcriptional repression activity, and also associates with ring finger protein 2 (RNF2) to form a RNF2-PCGF heterodimer, which is catalytically competent as an E3 ubiquitin transferase and is the scaffold for the assembly of additional components. Moreover, PCGF6 can regulate the enzymatic activity of JARID1d/KDM5D, a trimethyl H3K4 demethylase, through direct interaction. Furthermore, PCGF6 is expressed predominantly in meiotic and post-meiotic male germ cells and may play important roles in mammalian male germ cell development. It also regulates mesodermal lineage differentiation in mammalian embryonic stem cells (ESCs) and functions in induced pluripotent stem (iPS) reprogramming. The activity of PCGF6 is found to be regulated by cell cycle dependent phosphorylation. PCGF6 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438396 [Multi-domain]  Cd Length: 59  Bit Score: 40.67  E-value: 1.27e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 34878777 913 IKDYKARLTCPCCNMRKKDAV-LTKCFHVFCFECVKTRYDTRQRkCPKCN 961
Cdd:cd16738   1 LAELNPYILCSICKGYFIDATtITECLHTFCKSCIVRHFYYSNR-CPKCN 49
RING-HC_PCGF cd16525
RING finger, HC subclass, found in Polycomb Group RING finger homologs (PCGF1, 2, 3, 4, 5 and ...
920-961 1.27e-04

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: 40.28  E-value: 1.27e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 34878777 920 LTCPCCNMRKKDAV-LTKCFHVFCFECVkTRYDTRQRKCPKCN 961
Cdd:cd16525   1 LTCSLCKGYLIDATtITECLHSFCKSCI-VRHLETSKNCPVCD 42
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
920-964 1.48e-04

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: 40.43  E-value: 1.48e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 34878777 920 LTCPCCNMRKKDAVLTKCFHVFCFECVK---TRYDTRQRKCPKCNAAF 964
Cdd:cd16609   4 LTCSICLGLYQDPVTLPCQHSFCRACIEdhwRQKDEGSFSCPECRAPF 51
mRING-HC-C3HC3D_TRAF7 cd16644
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
918-958 1.56e-04

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: 40.03  E-value: 1.56e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 34878777 918 ARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDtrqRKCP 958
Cdd:cd16644   4 VKLYCPLCQRVFKDPVITSCGHTFCRRCALTAPG---EKCP 41
RING-HC_RAD16-like cd16567
RING finger, HC subclass, found in Saccharomyces cerevisiae DNA repair protein RAD16, ...
922-961 1.70e-04

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: 40.02  E-value: 1.70e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 34878777 922 CPCCNMRKKDAVLTKCFHVFCFECVK---TRYDTRQRKCPKCN 961
Cdd:cd16567   3 CGICHEEAEDPVVARCHHVFCRACVKeyiESAPGGKVTCPTCH 45
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
922-960 1.73e-04

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 404756 [Multi-domain]  Cd Length: 40  Bit Score: 39.73  E-value: 1.73e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 34878777   922 CPCCNMRKKDA-VLTKCFHVFCFECVKtRYDTRQRKCPKC 960
Cdd:pfam13923   2 CPICMDMLKDPsTTTPCGHVFCQDCIL-RALRAGNECPLC 40
RING-HC_TRIM9-like_C-I cd16576
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM9, TRIM67, and ...
920-961 1.92e-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: 39.70  E-value: 1.92e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 34878777 920 LTCPCCNMRKKDAVLTKCFHVFCFECVKtrydTRQRKCPKCN 961
Cdd:cd16576   4 LKCPVCGSLFTEPVILPCSHNLCLGCAL----NIQLTCPICH 41
RING-HC_TRIM62_C-IV cd16608
RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar ...
917-964 2.74e-04

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: 39.41  E-value: 2.74e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 34878777 917 KARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDT-RQRKCPKCNAAF 964
Cdd:cd16608   4 KDELLCSICLSIYQDPVSLGCEHYFCRQCITEHWSRsEHRDCPECRRTF 52
PTZ00121 PTZ00121
MAEBL; Provisional
498-898 3.24e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777   498 KRKLREAQSDLNKTRLRSGSALLQSQSSTEDPKDEPAELKPDSEDLSSQSSASKASQEDANEIKSKRDEEERERERREKE 577
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777   578 REREREREKEKEREREKQKLKESEKERDSAKDKEKGKHDDGRKKEAEIIKQLKIELKKAQESQK--EMKLLLDMYRSAPK 655
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKkaEEAKKADEAKKKAE 1480
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777   656 EQRDKVQLMAAEKKSKAELEDLRQRlkdledkekKENKKMADEdalrkIRAVEEqieylQKKLAMAKQEEEAllSEMDVT 735
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKA---------AEAKKKADE-----AKKAEE-----AKKADEAKKAEEA--KKADEA 1539
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777   736 GQAFEDMQEQNIRLMQQLREkddanfklmSERIKSNQIHKLLKEEKEELADQVLTLKTQVDAQLQVVRKLEEKEHLLQSN 815
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKK---------AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777   816 IGTGEKELGLRTQALemnkRKAMEAAQLADDLKAQLELAQKKLHDFQDEIVENSVTKEKDMfnfKRAQEDisrlRRKLET 895
Cdd:PTZ00121 1611 EAKKAEEAKIKAEEL----KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA---KKAEED----KKKAEE 1679

                  ...
gi 34878777   896 TKK 898
Cdd:PTZ00121 1680 AKK 1682
RING-HC_PEX2 cd16526
RING finger, HC subclass, found in peroxin-2 (PEX2) and similar proteins; PEX2, also known as ...
935-964 4.34e-04

RING finger, HC subclass, found in peroxin-2 (PEX2) and similar proteins; PEX2, also known as peroxisome biogenesis factor 2, 35 kDa peroxisomal membrane protein, peroxisomal membrane protein 3, peroxisome assembly factor 1 (PAF-1), or RING finger protein 72 (RNF72), is an integral peroxisomal membrane protein with two transmembrane regions and a C3HC4-type RING-HC finger within its cytoplasmically exposed C-terminus. It may be involved in the biogenesis of peroxisomes, as well as in peroxisomal matrix protein import. Mutations in the PEX2 gene are the primary defect in a subset of patients with Zellweger syndrome and related peroxisome biogenesis disorders. Moreover, PEX2 functions as an E3-ubiquitin ligase that mediates the UBC4-dependent polyubiquitination of PEX5, a key player in peroxisomal matrix protein import, to control PEX5 receptor recycling or degradation.


Pssm-ID: 438189 [Multi-domain]  Cd Length: 49  Bit Score: 38.90  E-value: 4.34e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 34878777 935 TKCFHVFCFECVKTRYDTRQR-KCPKCNAAF 964
Cdd:cd16526  18 TGCGHVYCYYCIKSNLLADDSfTCPRCGSPV 48
RING-HC_RNF5 cd16743
RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins; RNF5, ...
922-965 4.43e-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: 39.10  E-value: 4.43e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 34878777 922 CPCCNMRKKDAVLTKCFHVFCFECVKTRYDTR--QRKCPKCNAAFG 965
Cdd:cd16743   3 CNICLETARDAVVSLCGHLFCWPCLHQWLETRpeRQECPVCKAGIS 48
RING-HC_RNFT1 cd16741
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 ...
922-960 4.58e-04

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: 39.10  E-value: 4.58e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 34878777 922 CPCCNMRKKDAVLTKCFHVFCFECVKTRYDtRQRKCPKC 960
Cdd:cd16741  17 CAICQAEFRKPILLICQHVFCEECISLWFN-REKTCPLC 54
RING-HC_RING1 cd16739
RING finger, HC subclass, found in really interesting new gene 1 protein (RING1) and similar ...
918-960 4.59e-04

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: 39.68  E-value: 4.59e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 34878777 918 ARLTCPCC-NMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKC 960
Cdd:cd16739   2 SELMCPIClDMLKNTMTTKECLHRFCSDCIVTALRSGNKECPTC 45
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
54-898 5.49e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.19  E-value: 5.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777     54 KNRKLAEMLDQRQAIEDELREhiEKLERRQATDDASLLIVNRYWSQFDENIRIILKRYDLEQGLGDLLTERKALVVPEPE 133
Cdd:pfam02463  174 ALKKLIEETENLAELIIDLEE--LKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    134 pDSDSNQERKDDRERGEGQEPAFSFLATLASSSSEEMESQLQERVESSRRAVSQIVTVYDKLQEKVELLSRKLNSGDNLI 213
Cdd:pfam02463  252 -EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    214 ------VEEAVQELNSFLAQENMRLQELTDLLQEKHRTMSQEFSKLQSKVETAESRVSVLEsmIDDLQWDIDKIRKREQR 287
Cdd:pfam02463  331 kkekeeIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK--LKEEELELKSEEEKEAQ 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    288 LNRHLAEVLERVNSKGYKVYGAGSSLYGGTITINARKFEEMNAELEENKELAQNRLCELEKLRQDFEEVTTQNEKLKVEL 367
Cdd:pfam02463  409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL 488
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    368 RSAVEQVVKETPEYRCMQSQFSVLYNESLQLKAHLdeaRTLLHGTRGTHQHQVELIERDEVSLHKKLRTEVIQLEDTLAQ 447
Cdd:pfam02463  489 LLSRQKLEERSQKESKARSGLKVLLALIKDGVGGR---IISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQK 565
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    448 VRKEYEMLRIEFEQTLAANEQAGPINREMRHLISSL-----QNHNHQLKGEVLRYKRKLREAQSDLNKTRLRSGSALLQS 522
Cdd:pfam02463  566 LVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPilnlaQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE 645
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    523 QSSTEDPKDEPAELKPDSEDLSSQSSASKASQEDANEIKSKRDEEERERERREKEREREREREKEKEREREKQKLKESEK 602
Cdd:pfam02463  646 SGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLAD 725
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    603 ERDSAKDKEKGKHDDGRKKEAEIIKQLKIELKKAQESQKEMKLLLDMYRSAPKEQRDKVQLMAAEKKSKAELEDLRQRLK 682
Cdd:pfam02463  726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRA 805
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    683 DLEDKEKKENKKMADEDALRKIRAVEEQIEYLQKKLAMAKQEEEALLSEMDVTGQAFEDMQEQNIRLMQQLREKDDanfk 762
Cdd:pfam02463  806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEE---- 881
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    763 lmsERIKSNQIHKLLKEEKEELADQVLTLKTQVDAQLQVVRKLEEKE--HLLQSNIGTGEKELGLRTQALEMNKRKAMEA 840
Cdd:pfam02463  882 ---QKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEeaEILLKYEEEPEELLLEEADEKEKEENNKEEE 958
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 34878777    841 AQLADDLKAQLELAQKKLHDFQDEIVENSVTKEKDMFNFKRAQEDISRLRRKLETTKK 898
Cdd:pfam02463  959 EERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
RING-HC_RNF166 cd16549
RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins; ...
920-964 5.64e-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: 38.64  E-value: 5.64e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 34878777 920 LTCPCC-NMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAF 964
Cdd:cd16549   2 FSCPIClEVYHKPVVITSCGHTFCGECLQPCLQVASPLCPLCRMPF 47
RING-HC_RNF222 cd16564
RING finger, HC subclass, found in RING finger protein 222 (RNF222) and similar proteins; ...
921-961 6.27e-04

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: 38.54  E-value: 6.27e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 34878777 921 TCPCC--NMRKKDAVLTkCFHVFCFECVKTRYDTRQRKCPKCN 961
Cdd:cd16564   2 ECPVCyeDFDDAPRILS-CGHSFCEDCLVKQLVSMTISCPICR 43
mRING-C3HGC3_RFWD3 cd16450
Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing ...
936-973 7.15e-04

Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing protein 3 (RFWD3) and similar proteins; RFWD3, also known as RING finger protein 201 (RNF201) or FLJ10520, is an E3 ubiquitin-protein ligase that forms a complex with Mdm2 and p53 to synergistically ubiquitinate p53 and acts as a positive regulator of p53 stability in response to DNA damage. It is phosphorylated by checkpoint kinase ATM/ATR and the phosphorylation mutant fails to stimulate p53 ubiquitination. RFWD3 also functions as a novel replication protein A (RPA)-associated protein involved in DNA replication checkpoint control. RFWD3 contains an N-terminal SQ-rich region followed by a RING finger domain that exhibits robust E3 ubiquitin ligase activity toward p53, a coiled-coil domain and three WD40 repeats in the C-terminus, the latter two of which may be responsible for protein-protein interaction. The RING finger in this family is a modified C3HGC3-type RING finger, but not a canonical C3H2C3-type RING-H2 finger or C3HC4-type RING-HC finger.


Pssm-ID: 438114 [Multi-domain]  Cd Length: 61  Bit Score: 38.75  E-value: 7.15e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 34878777 936 KCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIY 973
Cdd:cd16450  24 KCGHLFGYSCIEKWLKGKGKKCPQCNKKAKRSDIRPLY 61
RING-HC_RNF151 cd16547
RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins; ...
920-960 7.30e-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: 38.21  E-value: 7.30e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 34878777 920 LTCPCCNMRKKDAVLTKCFHVFCFECVkTRYDTRQRKCPKC 960
Cdd:cd16547   4 LICSICHGVLRCPVRLSCSHIFCKKCI-LQWLKRQETCPCC 43
RING-HC_RNF125 cd16542
RING finger, HC subclass, found in RING finger protein 125 (RNF125); RNF125, also known as ...
920-962 7.64e-04

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: 38.32  E-value: 7.64e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 34878777 920 LTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNA 962
Cdd:cd16542   2 FDCAVCLEVLHQPVRTRCGHVFCRPCIATSLRNNTWTCPYCRA 44
RING-HC_AtRMA-like cd16745
RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) ...
922-962 8.32e-04

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: 37.85  E-value: 8.32e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 34878777 922 CPCCNMRKKDAVLTKCFHVFCFECVK--TRYDTRQRKCPKCNA 962
Cdd:cd16745   3 CNICLDLAQDPVVTLCGHLFCWPCLHkwLRRQSSQPECPVCKA 45
RING-HC_RNF113A_B cd16539
RING finger, HC subclass, found in RING finger proteins RNF113A, RNF113B, and similar proteins; ...
921-963 8.33e-04

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: 38.34  E-value: 8.33e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 34878777 921 TCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQrKCPKCNAA 963
Cdd:cd16539   7 ACFICRKPFKNPVVTKCGHYFCEKCALKHYRKSK-KCFVCGKQ 48
RING-HC_ScPSH1-like cd16568
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated ...
916-960 8.80e-04

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: 38.12  E-value: 8.80e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 34878777 916 YKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRY-DTRQRKCPKC 960
Cdd:cd16568   1 ILETQECIICHEYLYEPMVTTCGHTYCYTCLNTWFkSNRSLSCPDC 46
RING-HC_ORTHRUS_rpt1 cd23138
first RING finger, HC subclass, found in Arabidopsis thaliana ORTHRUS and similar proteins; ...
920-964 9.48e-04

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: 37.81  E-value: 9.48e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 34878777 920 LTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAF 964
Cdd:cd23138   3 LNCSFCMQLPERPVTTPCGHNFCLKCFQKWMGQGKKTCGTCRSPI 47
RING-HC_PRT1-like cd23132
RING finger, HC subclass, found in Arabidopsis thaliana proteolysis 1 protein (PRT1) and ...
920-965 1.00e-03

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: 38.17  E-value: 1.00e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 34878777 920 LTCPCC-NMRKKDAVLTkCFHVFCFECV-KTRYDTRQRKCPKCNAAFG 965
Cdd:cd23132   3 FLCCIClDLLYKPVVLE-CGHVFCFWCVhRCMNGYDESHCPLCRRPYD 49
RING-HC_TRIM35_C-IV cd16599
RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar ...
916-963 1.01e-03

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


Pssm-ID: 438261 [Multi-domain]  Cd Length: 66  Bit Score: 38.60  E-value: 1.01e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 34878777 916 YKARLTCPCCNMRKKDAVLTKCFHVFCFECVKtRYDTRQRK--CPKCNAA 963
Cdd:cd16599   1 FKEELLCPICYEPFREAVTLRCGHNFCKGCVS-RSWERQPRapCPVCKEA 49
mRING-HC-C3HC3D_TRAF6 cd16643
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
919-968 1.01e-03

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: 38.13  E-value: 1.01e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 34878777 919 RLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGAND 968
Cdd:cd16643   1 KYECPICLMALREPVQTPCGHRFCKACILKSIREAGHKCPVDNEPLLENQ 50
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
655-899 1.04e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 655 KEQRDKVQLMAAEKKSKAELEDLRQRLKDLEDKEKKENKKMADEDAlrKIRAVEEQIEYLQKKLAMAKQEEEALLSEMDV 734
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA--ELEELRLELEELELELEEAQAEEYELLAELAR 299
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 735 TGQAFEDMQEQNIRLMQQLREKDDANFKLMSERIKSNQIHKLLKEEKEELADQVLTLKTQVDAQLQVVRKLEEKEHLLQS 814
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 815 NIGTGEKELGLRTQALEMNKRKAMEAAQLADDLKAQLELAQKKLHDFQDEIVENSVTKEKDMFNFKRAQEDISRLRRKLE 894
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459

                ....*
gi 34878777 895 TTKKP 899
Cdd:COG1196 460 ALLEL 464
RING-HC_RAD18 cd16529
RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; ...
918-963 1.18e-03

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: 37.67  E-value: 1.18e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 34878777 918 ARLTCPCC-NMRKKDAVLTKCFHVFCFECVKtRYDTRQRKCPKCNAA 963
Cdd:cd16529   3 DLLRCPICfEYFNTAMMITQCSHNYCSLCIR-RFLSYKTQCPTCRAA 48
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
177-461 1.33e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    177 RVESSRRAVSQIVTVYDKLQEKVELLSRKLNSgdnliVEEAVQELNSFLAQENMRLQELTDllqEKHRTMSQEFSKLQSK 256
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISE-----LEKRLEEIEQLLEELNKKIKDLGE---EEQLRVKEKIGELEAE 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    257 VETAESRVSVLESMIDDLQwdiDKIRKREQRLNRHLAEVLERvnskgykvygagsslyggtitinARKFEEMNAELEENK 336
Cdd:TIGR02169  303 IASLERSIAEKERELEDAE---ERLAKLEAEIDKLLAEIEEL-----------------------EREIEEERKRRDKLT 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    337 ELAQNRLCELEKLRQDFEEVTTQNEKLKVELRSAVEQVVKETPEYRCMQSQFSVLYNESLQLKAHLDEARTLLHGTRGTH 416
Cdd:TIGR02169  357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 34878777    417 QhqvELIERDEVSLH--KKLRTEVIQLEDTLAQVRKEYEMLRIEFEQ 461
Cdd:TIGR02169  437 N---ELEEEKEDKALeiKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
mRING_PEX12 cd16451
Modified RING finger found in peroxin-12 (PEX12) and similar proteins; PEX12, also known as ...
921-958 1.39e-03

Modified RING finger found in peroxin-12 (PEX12) and similar proteins; PEX12, also known as peroxisome assembly protein 12 or peroxisome assembly factor 3 (PAF-3), is a RING finger domain-containing integral membrane peroxin required for protein import into peroxisomes. Mutations in human PEX12 result in the peroxisome deficiency Zellweger syndrome of complementation group III (CG-III), a lethal neurological disorder. PEX12 also functions as an E3-ubiquitin ligase that facilitates the PEX4-dependent monoubiquitination of PEX5, a key player in peroxisomal matrix protein import, to control PEX5 receptor recycling or degradation. PEX12 contains a modified RING finger that lacks the third, fourth, and eighth zinc-binding residues of the consensus RING finger motif, suggesting PEX12 may only bind one zinc ion.


Pssm-ID: 438115 [Multi-domain]  Cd Length: 54  Bit Score: 37.61  E-value: 1.39e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 34878777 921 TCPCC-NMRKKDAVLTKCFHVFCFECVkTRYDTRQRKCP 958
Cdd:cd16451   2 ICPLCrKKRTNPTALATSGYVFCYPCI-YRYVKEHGRCP 39
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
231-779 1.49e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 1.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 231 RLQELTDLLQEKHRTMSQEFSKLQSKVETAESRVSVLESMIDDLQWDIDKIRKREQRLNRHLAEVLERVNskgykvygag 310
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA---------- 305
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 311 ssLYGGTITINARKFEEMNAELEENKELAQNRLCELEKLRQDFEEVTTQNEKLKVELRSAVEQVVKETPEYRCMQSQFSV 390
Cdd:COG1196 306 --RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 391 LYNESLQLKAHLDEARTLLHGTRGTHQHQVELIERDEVSLhKKLRTEVIQLEDTLAQVRKEYEMLRIEFEQTLAANEQAG 470
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL-EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 471 PINREMRHLISSLQNHNHQLKGEVLRYKRKLREAQSDLNKTRLRSGSALLQSQSS---------TEDPKDEPAELKPDSE 541
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrglagavAVLIGVEAAYEAALEA 542
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 542 DLSSQSSASKASQED-----ANEIKSKRDEEERERERREKEREREREREKEKEREREKQKLKESEKERDSAKDKEKGKHD 616
Cdd:COG1196 543 ALAAALQNIVVEDDEvaaaaIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 617 DGRKKEAEIIKQLKIELKKAQESQKEMKLLLDMYRSAPKEQRDKVQLMAAEKKSKAELEDLRQRLKDLEDKEKKENKKMA 696
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 697 DEDALRKIRAVEEQIEYLQKKLAMAKQEEEALLSEmdvtgQAFEDMQEQNIRLMQQLREKDDANFKLMSERIKSNQihkl 776
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREEL-----LEELLEEEELLEEEALEELPEPPDLEELERELERLE---- 773

                ...
gi 34878777 777 lkE 779
Cdd:COG1196 774 --R 774
RING-HC_RING1-like cd16531
RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and ...
920-960 1.53e-03

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: 38.02  E-value: 1.53e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 34878777 920 LTCPCCNMRKKDAVLTK-CFHVFCFECVKTRYDTRQRKCPKC 960
Cdd:cd16531   2 LMCPICLGIIKNTMTVKeCLHRFCAECIEKALRLGNKECPTC 43
RING-HC_TRIM25_C-IV cd16597
RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar ...
908-964 1.75e-03

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


Pssm-ID: 438259 [Multi-domain]  Cd Length: 71  Bit Score: 38.06  E-value: 1.75e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 908 ILMEEikdykarLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDT---RQRKCPKCNAAF 964
Cdd:cd16597   1 DLEEE-------LTCSICLELFKDPVTLPCGHNFCGVCIEKTWDSqhgSEYSCPQCRATF 53
RING-HC_TRIM47-like_C-IV cd16604
RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar ...
920-964 2.01e-03

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: 37.02  E-value: 2.01e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 34878777 920 LTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRK---CPKCNAAF 964
Cdd:cd16604   1 LSCPICLDLLKDPVTLPCGHSFCMGCLGALWGAGRGGrasCPLCRQTF 48
RING-HC_RNF213 cd16561
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ...
922-963 2.30e-03

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: 36.87  E-value: 2.30e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 34878777 922 CPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRkCPKCNAA 963
Cdd:cd16561   5 CSICLEDLNDPVKLPCDHVFCEECIRQWLPGQMS-CPLCRTE 45
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
256-573 2.47e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 2.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    256 KVETAESRVSVLESMIDDLQWDIDKIRKREQRLNRHLAEVLERVNSKGYKVYGAGSSLYGGTITINARkFEEMNAELEEN 335
Cdd:TIGR02169  178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQ-LASLEEELEKL 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    336 KELAQNRLCELEKLRQDFEEVTTQNEKLKVELRSAV-EQVVKETPEYRCMQSQFSVLYNESLQLKAHLDEARTLLHGTRG 414
Cdd:TIGR02169  257 TEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    415 THQHQVELIERdevslhkkLRTEVIQLEDTLAQVRKEYEMLRIEFEQTLAANEQAGPINREMRHLISSLQNHNHQLKGEV 494
Cdd:TIGR02169  337 EIEELEREIEE--------ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777    495 LRY---KRKLREAQSDLNKTRLRSGSALLQSQSSTEDPKDEPA----ELKPDSEDLSSQSSASKASQEDANEIKSKRDEE 567
Cdd:TIGR02169  409 DRLqeeLQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKkqewKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488

                   ....*.
gi 34878777    568 ERERER 573
Cdd:TIGR02169  489 QRELAE 494
RING-HC_RING2 cd16740
RING finger, HC subclass, found in really interesting new gene 2 protein (RING2) and similar ...
914-960 2.75e-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: 37.76  E-value: 2.75e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 34878777 914 KDYKARLTCPCC-NMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKC 960
Cdd:cd16740   7 RSLHSELMCPIClDMLKNTMTTKECLHRFCADCIITALRSGNKECPTC 54
RING-HC_PCGF1 cd16733
RING finger, HC subclass, found in polycomb group RING finger protein 1 (PCGF1) and similar ...
913-961 2.86e-03

RING finger, HC subclass, found in polycomb group RING finger protein 1 (PCGF1) and similar proteins; PCGF1, also known as nervous system Polycomb-1 (NSPc1) or RING finger protein 68 (RNF68), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR). It serves as the core component of a noncanonical Polycomb repressive complex 1 (PRC1)-like BCOR complex that also contains RING1, RNF2, RYBP, SKP1, as well as the BCL6 co-repressor BCOR and the histone demethylase KDM2B, and is required to maintain the transcriptionally repressive state of some genes, such as Hox genes, BCL6 and the cyclin-dependent kinase inhibitor, CDKN1A. PCGF1 promotes cell cycle progression and enhances cell proliferation as well. It is a cell growth regulator that acts as a transcriptional repressor of p21Waf1/Cip1 via the retinoid acid response element (RARE element). Moreover, PCGF1 functions as an epigenetic regulator involved in hematopoietic cell differentiation. It cooperates with the transcription factor runt-related transcription factor 1 (Runx1) in regulating differentiation and self-renewal of hematopoietic cells. Furthermore, PCGF1 represents a physical and functional link between Polycomb function and pluripotency. PCGF1 contains a C3HC4-type RING-HC finger.


Pssm-ID: 438391 [Multi-domain]  Cd Length: 71  Bit Score: 37.25  E-value: 2.86e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 34878777 913 IKDYKARLTCPCCNMRKKDAV-LTKCFHVFCFECVkTRYDTRQRKCPKCN 961
Cdd:cd16733   3 IKDLNEHIVCYLCAGYFIDATtITECLHTFCKSCI-VKYLQTSKYCPMCN 51
RING-HC_RNF208 cd16559
RING finger, HC subclass, found in RING finger protein 208 (RNF208) and similar proteins; ...
920-960 2.93e-03

RING finger, HC subclass, found in RING finger protein 208 (RNF208) and similar proteins; RNF208 is an E3 ubiquitin-protein ligase whose activity can be modulated by S-nitrosylation. It contains a C3HC4-type RING-HC finger.


Pssm-ID: 438221 [Multi-domain]  Cd Length: 56  Bit Score: 36.83  E-value: 2.93e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 34878777 920 LTCPCCNMR----KKDAVLTKCFHVFCFECVKTRYDTRQRK----CPKC 960
Cdd:cd16559   2 LLCPTCGHSynftNKRPRILSCLHSVCEECLQILYESCPKYkfisCPTC 50
RING-HC_PEX10 cd16527
RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known ...
922-964 3.01e-03

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: 36.44  E-value: 3.01e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 34878777 922 CPCCNMRKKDAVLTKCFHVFCFECVkTRYDTRQRKCPKCNAAF 964
Cdd:cd16527   3 CSLCLEERRHPTATPCGHLFCWSCI-TEWCNEKPECPLCREPF 44
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
215-382 3.02e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 3.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 215 EEAVQELNSfLAQENMRLQELTDLLQEKHRTMSQEFSKLQSKVETAESRVSVLESMIDDLQWDIDKIRKREQRLNRHLAE 294
Cdd:COG4942  23 AEAEAELEQ-LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 295 VLERVNSKGYKVYGAGS--------------------SLYGGTITINARKFEEMNA---ELEENKELAQNRLCELEKLRQ 351
Cdd:COG4942 102 QKEELAELLRALYRLGRqpplalllspedfldavrrlQYLKYLAPARREQAEELRAdlaELAALRAELEAERAELEALLA 181
                       170       180       190
                ....*....|....*....|....*....|.
gi 34878777 352 DFEEVTTQNEKLKVELRSAVEQVVKETPEYR 382
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELA 212
RING-HC_TRIM39_C-IV cd16601
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ...
922-960 3.26e-03

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: 36.31  E-value: 3.26e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 34878777 922 CPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRK--CPKC 960
Cdd:cd16601   4 CSLCKEYLKDPVIIECGHNFCRACITRFWEELDGDfpCPQC 44
RING-HC_RNF146 cd16546
RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins; ...
920-969 3.63e-03

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


Pssm-ID: 438208 [Multi-domain]  Cd Length: 50  Bit Score: 36.21  E-value: 3.63e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 34878777 920 LTCPCCNMRKKDAVLTKCFHVFCFECVKTRYdTRQRKCPKCNAAFgANDF 969
Cdd:cd16546   1 PECPICLQTCIHPVKLPCGHIFCYLCVKGVA-WQSKRCALCRQEI-PEDF 48
46 PHA02562
endonuclease subunit; Provisional
174-378 4.43e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 40.77  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777  174 LQERVESSRRAVSQIVTVYDKLQEKVELLSRKLNSgdnliVEEAVQELNSFLAQENMRLQELTDLLQ--EKHR---TMSQ 248
Cdd:PHA02562 218 KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIED-----PSAALNKLNTAAAKIKSKIEQFQKVIKmyEKGGvcpTCTQ 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777  249 EFSKLQSKVETAESRVSVLESMIDDLQWDIDKIRKREQRLNRHLAEVLErVNSKgykvygagSSLYGGTITINARKFEEM 328
Cdd:PHA02562 293 QISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE-LKNK--------ISTNKQSLITLVDKAKKV 363
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 34878777  329 NAELEENKELAQNRLCELEKLRQDFEEVTTQNEKLKVEL--RSAVEQVVKET 378
Cdd:PHA02562 364 KAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKyhRGIVTDLLKDS 415
RING-HC_RAD5 cd23131
RING finger, HC subclass, found in radiation sensitivity protein 5 (RAD5) and similar proteins; ...
922-967 5.13e-03

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: 36.27  E-value: 5.13e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 34878777 922 CPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRK-----CPKCNAAFGAN 967
Cdd:cd23131   9 CTQEPIEVGEVVFTECGHSFCEDCLLEYIEFQNKKkldlkCPNCREPISKY 59
RING-HC_ScRAD18-like cd23148
RING finger, HC subclass, found in Saccharomyces cerevisiae radiation sensitivity protein 18 ...
920-964 5.41e-03

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: 35.97  E-value: 5.41e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 34878777 920 LTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDtRQRKCPKCNAAF 964
Cdd:cd23148   4 LRCHICKDLLKAPMRTPCNHTFCSFCIRTHLN-NDARCPLCKAEV 47
RING_Ubox cd00162
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ...
922-960 7.09e-03

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.


Pssm-ID: 438111 [Multi-domain]  Cd Length: 42  Bit Score: 35.13  E-value: 7.09e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 34878777 922 CPCCNMRKKDA---VLTKCFHVFCFECVKTRYDTRQRKCPKC 960
Cdd:cd00162   1 CPICREEMNDRrpvVLLSCGHTFSRSAIARWLEGSKQKCPFC 42
mRING-HC-C3HC3D_LNX1-like cd16637
Modified RING finger, HC subclass (C3HC3D-type), found in ligand of Numb protein LNX1, LNX2, ...
919-958 8.10e-03

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: 35.07  E-value: 8.10e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 34878777 919 RLTCPCCNMRKKDAVLTKCFHVFCFECVKTrYDTRQRKCP 958
Cdd:cd16637   1 DLTCHICLQPLVEPLDTPCGHTFCYKCLTN-YLKIQQCCP 39
RING-HC_EHV1-like cd23130
RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) ...
922-964 8.88e-03

RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) regulatory protein and similar proteins; EHV-1 regulatory protein belongs to the Vmw110 (IPC0) protein family. It contains a typical C3HC4-type RING-HC finger and binds zinc stably.


Pssm-ID: 438492 [Multi-domain]  Cd Length: 51  Bit Score: 35.41  E-value: 8.88e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 34878777 922 CPCC-NMRKKDAVLTKCFHVFCFECVKtRYDTRQRKCPKCNAAF 964
Cdd:cd23130   3 CPIClDDPEDEAITLPCLHQFCYTCIL-RWLQTSPTCPLCKTPV 45
RING-HC_DTX3-like cd16506
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like ...
921-961 9.83e-03

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


Pssm-ID: 438169 [Multi-domain]  Cd Length: 45  Bit Score: 35.03  E-value: 9.83e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 34878777 921 TCPCC--NMRKKDaVLTKCFHVFCFECVKTRYDTRQrKCPKCN 961
Cdd:cd16506   2 TCPICldEIQNKK-TLEKCKHSFCEDCIDRALQVKP-VCPVCG 42
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
173-298 9.87e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 9.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878777 173 QLQERVESSRRAVSQIVTVYDKLQEKVELLSRKLNSGDNLIVE----EAVQELNSFLAQENMRLQELTDLLQEKHRTM-- 246
Cdd:COG3206 216 LLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEllqsPVIQQLRAQLAELEAELAELSARYTPNHPDVia 295
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34878777 247 ----------------SQEFSKLQSKVETAESRVSVLESMIDDLQWDIDKIRKREQRLNRhlaevLER 298
Cdd:COG3206 296 lraqiaalraqlqqeaQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR-----LER 358
 
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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