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Conserved domains on  [gi|122692531|ref|NP_001073722|]
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RING finger protein unkempt homolog [Bos taurus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RING-HC_UNK cd16771
RING finger, HC subclass, found in RING finger protein unkempt (UNK) and similar proteins; UNK, ...
 765-806 7.12e-18

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


:

Pssm-ID: 438427  Cd Length: 42  Bit Score: 77.56  E-value: 7.12e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 122692531 765 QSVKCLKCQEQNRAVLPCQHAVLCELCAEGSECPVCQPGRAH 806
Cdd:cd16771    1 QSVKCLKCQELKRVTLPCQHALLCETCATSEECPICHPHRPH 42
zf_CCCH_5 pfam18384
Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt ...
 34-69 3.98e-16

Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt N-terminal region. Unkempt is an evolutionary conserved RNA-binding protein that regulates translation of its target genes and is required for the establishment of the early bipolar neuronal morphology. It carries six CCCH zinc fingers (ZnFs) forming two compact clusters, ZnF1-3 and ZnF4-6, that recognize distinct trinucleotide RNA substrates. These clusters, recognize an unexpectedly short stretch of RNA sequence-only three consecutive ribonucleotides-with a varying degree of specificity. ZnF1-3 binds to the UUA motif of RNA substrates.


:

Pssm-ID: 375810  Cd Length: 40  Bit Score: 72.58  E-value: 3.98e-16
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 122692531   34 YTYLKEFRTEQCPLFVQHKCTQHRPYTCFHWHFVNQ 69
Cdd:pfam18384   1 YHYLKNFRVRQCPRFLQHHCPAHKPMTCFDWHFDNQ 36
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
643-722 1.63e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531  643 GAAELARLRQELDEANGTIKQWEESWKQAKQAC-----------DAWKKEAEEAGERASAAGAECELAREQRDALEVQVK 711
Cdd:COG4913   336 GGDRLEQLEREIERLERELEERERRRARLEALLaalglplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415

                          90
                  ....*....|.
gi 122692531  712 KLQEELERLHS 722
Cdd:COG4913   416 DLRRELRELEA 426
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
294-320 1.55e-03

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


:

Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 36.40  E-value: 1.55e-03
                          10        20
                  ....*....|....*....|....*..
gi 122692531  294 YKSTKCNDMQQSGSCPRGPFCAFAHVE 320
Cdd:pfam00642   1 YKTELCRFFLRTGYCKYGDRCKFAHGQ 27
CTH1 super family cl34885
CCCH-type Zn-finger protein [General function prediction only];
124-318 5.51e-03

CCCH-type Zn-finger protein [General function prediction only];


The actual alignment was detected with superfamily member COG5063:

Pssm-ID: 227395 [Multi-domain]  Cd Length: 351  Bit Score: 40.04  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531 124 YYKTGICIHETDaKGNCTkNGLHCAFAHGPHDLR-SPVYDIRELQAMEALQNGQTTVEGSMEGQSAGAASHAMIEKILSE 202
Cdd:COG5063  112 LYKTEMLRSSTE-IPYCR-YPDKNPFAHSKAISSlAQTHPKYKTESLEVFINPGYVPYSKRCCFISLPLTDINLQPLSQR 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531 203 EPR--WQETAYVLG-NYKTEPC---------------KKPPRLC----RQGYaCPYYHNSKDRRRSPRKH---------- 250
Cdd:COG5063  190 KPKsgKNCTSYTLGkESDAHPHdeliyqkqeqnkplyKTNPELCesftRKGT-CPYWISGVKCQFACRGHglnelkskkk 268

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 122692531 251 --KYRSSPCPNvkhgdeWGDPGKCENGDSCQYCHTRTEQQFHPE----IYKSTKCNDMQQSGSCPRGPFCAFAH 318
Cdd:COG5063  269 kqNFRTEPCIN------WEKSGYCPYGLRCCFKHGDDSDIEMYEeaslGYLDGPCRTRAKGGAFPSGGAVCKSF 336
 
Name Accession Description Interval E-value
RING-HC_UNK cd16771
RING finger, HC subclass, found in RING finger protein unkempt (UNK) and similar proteins; UNK, ...
 765-806 7.12e-18

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


Pssm-ID: 438427  Cd Length: 42  Bit Score: 77.56  E-value: 7.12e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 122692531 765 QSVKCLKCQEQNRAVLPCQHAVLCELCAEGSECPVCQPGRAH 806
Cdd:cd16771    1 QSVKCLKCQELKRVTLPCQHALLCETCATSEECPICHPHRPH 42
zf_CCCH_5 pfam18384
Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt ...
 34-69 3.98e-16

Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt N-terminal region. Unkempt is an evolutionary conserved RNA-binding protein that regulates translation of its target genes and is required for the establishment of the early bipolar neuronal morphology. It carries six CCCH zinc fingers (ZnFs) forming two compact clusters, ZnF1-3 and ZnF4-6, that recognize distinct trinucleotide RNA substrates. These clusters, recognize an unexpectedly short stretch of RNA sequence-only three consecutive ribonucleotides-with a varying degree of specificity. ZnF1-3 binds to the UUA motif of RNA substrates.


Pssm-ID: 375810  Cd Length: 40  Bit Score: 72.58  E-value: 3.98e-16
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 122692531   34 YTYLKEFRTEQCPLFVQHKCTQHRPYTCFHWHFVNQ 69
Cdd:pfam18384   1 YHYLKNFRVRQCPRFLQHHCPAHKPMTCFDWHFDNQ 36
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
643-722 1.63e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531  643 GAAELARLRQELDEANGTIKQWEESWKQAKQAC-----------DAWKKEAEEAGERASAAGAECELAREQRDALEVQVK 711
Cdd:COG4913   336 GGDRLEQLEREIERLERELEERERRRARLEALLaalglplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415

                          90
                  ....*....|.
gi 122692531  712 KLQEELERLHS 722
Cdd:COG4913   416 DLRRELRELEA 426
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 620-712 7.29e-06

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 49.95  E-value: 7.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531  620 SIWEH--------FASGSFSPGTSPAFLSGPGAAELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASA 691
Cdd:PRK11448  116 AVWFHrtygkdwdFKPGPFVPPEDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQE 195

                          90       100
                  ....*....|....*....|.
gi 122692531  692 AGAECELAREQRDALEVQVKK 712
Cdd:PRK11448  196 LEAQLEQLQEKAAETSQERKQ 216
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
644-802 1.72e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531 644 AAELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLH-- 721
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRer 399

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531 722 ---SGPDPQALPAFPGLEALSLSTLHSLQKRLRAHLEQVDKAVfhmqsvkclkcqEQNRAVLpcqhavlcelcAEGsECP 798
Cdd:PRK02224 400 fgdAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV------------EEAEALL-----------EAG-KCP 455


                 ....*
gi 122692531 799 VC-QP 802
Cdd:PRK02224 456 ECgQP 460
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 645-722 8.59e-05

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 44.67  E-value: 8.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531  645 AELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGErasaAGAEcELARE---QRDALEVQVKKLQEELERLH 721
Cdd:pfam04012  36 SELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALT----KGNE-ELAREalaEKKSLEKQAEALETQLAQQR 110


                  .
gi 122692531  722 S 722
Cdd:pfam04012 111 S 111
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
768-801 1.28e-04

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 40.05  E-value: 1.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 122692531  768 KCLKCQEQNR--AVLPCQHAVLCELCAE-----GSECPVCQ 801
Cdd:pfam13920   4 LCVICLDRPRnvVLLPCGHLCLCEECAErllrkKKKCPICR 44
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 645-793 1.70e-04

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: 45.43  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531   645 AELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLHSgp 724
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS-- 386

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 122692531   725 dpqalpAFPGLEaLSLSTLHSLQKRLRAHLEQVDKAVFHMQSVKCLKCQEQNRAVLPCQHAVLCELCAE 793
Cdd:TIGR02168  387 ------KVAQLE-LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE 448
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
294-320 1.55e-03

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 36.40  E-value: 1.55e-03
                          10        20
                  ....*....|....*....|....*..
gi 122692531  294 YKSTKCNDMQQSGSCPRGPFCAFAHVE 320
Cdd:pfam00642   1 YKTELCRFFLRTGYCKYGDRCKFAHGQ 27
CTH1 COG5063
CCCH-type Zn-finger protein [General function prediction only];
124-318 5.51e-03

CCCH-type Zn-finger protein [General function prediction only];


Pssm-ID: 227395 [Multi-domain]  Cd Length: 351  Bit Score: 40.04  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531 124 YYKTGICIHETDaKGNCTkNGLHCAFAHGPHDLR-SPVYDIRELQAMEALQNGQTTVEGSMEGQSAGAASHAMIEKILSE 202
Cdd:COG5063  112 LYKTEMLRSSTE-IPYCR-YPDKNPFAHSKAISSlAQTHPKYKTESLEVFINPGYVPYSKRCCFISLPLTDINLQPLSQR 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531 203 EPR--WQETAYVLG-NYKTEPC---------------KKPPRLC----RQGYaCPYYHNSKDRRRSPRKH---------- 250
Cdd:COG5063  190 KPKsgKNCTSYTLGkESDAHPHdeliyqkqeqnkplyKTNPELCesftRKGT-CPYWISGVKCQFACRGHglnelkskkk 268

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 122692531 251 --KYRSSPCPNvkhgdeWGDPGKCENGDSCQYCHTRTEQQFHPE----IYKSTKCNDMQQSGSCPRGPFCAFAH 318
Cdd:COG5063  269 kqNFRTEPCIN------WEKSGYCPYGLRCCFKHGDDSDIEMYEeaslGYLDGPCRTRAKGGAFPSGGAVCKSF 336
 
Name Accession Description Interval E-value
RING-HC_UNK cd16771
RING finger, HC subclass, found in RING finger protein unkempt (UNK) and similar proteins; UNK, ...
 765-806 7.12e-18

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


Pssm-ID: 438427  Cd Length: 42  Bit Score: 77.56  E-value: 7.12e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 122692531 765 QSVKCLKCQEQNRAVLPCQHAVLCELCAEGSECPVCQPGRAH 806
Cdd:cd16771    1 QSVKCLKCQELKRVTLPCQHALLCETCATSEECPICHPHRPH 42
zf_CCCH_5 pfam18384
Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt ...
 34-69 3.98e-16

Unkempt Zinc finger domain 1 (Znf1); This is CCCH zinc finger 1 domain found in Unkempt N-terminal region. Unkempt is an evolutionary conserved RNA-binding protein that regulates translation of its target genes and is required for the establishment of the early bipolar neuronal morphology. It carries six CCCH zinc fingers (ZnFs) forming two compact clusters, ZnF1-3 and ZnF4-6, that recognize distinct trinucleotide RNA substrates. These clusters, recognize an unexpectedly short stretch of RNA sequence-only three consecutive ribonucleotides-with a varying degree of specificity. ZnF1-3 binds to the UUA motif of RNA substrates.


Pssm-ID: 375810  Cd Length: 40  Bit Score: 72.58  E-value: 3.98e-16
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 122692531   34 YTYLKEFRTEQCPLFVQHKCTQHRPYTCFHWHFVNQ 69
Cdd:pfam18384   1 YHYLKNFRVRQCPRFLQHHCPAHKPMTCFDWHFDNQ 36
RING-HC_UNK-like cd16614
RING finger, HC subclass, found in RING finger protein unkempt (UNK), unkempt-like (UNKL), and ...
 767-801 4.83e-10

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


Pssm-ID: 438276  Cd Length: 38  Bit Score: 55.26  E-value: 4.83e-10
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 122692531 767 VKCLKCQEQNR--AVLPCQHAVLCELCAEGS-ECPVCQ 801
Cdd:cd16614    1 KKCMKCEERNRsvAVLPCQHYVLCEQCAETAtECPYCH 38
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
643-722 1.63e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531  643 GAAELARLRQELDEANGTIKQWEESWKQAKQAC-----------DAWKKEAEEAGERASAAGAECELAREQRDALEVQVK 711
Cdd:COG4913   336 GGDRLEQLEREIERLERELEERERRRARLEALLaalglplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415

                          90
                  ....*....|.
gi 122692531  712 KLQEELERLHS 722
Cdd:COG4913   416 DLRRELRELEA 426
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
645-720 1.75e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 1.75e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 122692531 645 AELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERL 720
Cdd:COG4372   45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
RING-HC_UNKL cd16772
RING finger, HC subclass, found in RING finger protein unkempt-like (UNKL) and similar ...
 768-801 5.31e-06

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


Pssm-ID: 438428  Cd Length: 44  Bit Score: 44.01  E-value: 5.31e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 122692531 768 KCLKCQEQNRAVL--PCQHAVLCELCAEGS-ECPVCQ 801
Cdd:cd16772    2 KCIVCQERDRSIVlqPCQHYVLCEHCAASKpECPYCK 38
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 620-712 7.29e-06

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 49.95  E-value: 7.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531  620 SIWEH--------FASGSFSPGTSPAFLSGPGAAELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASA 691
Cdd:PRK11448  116 AVWFHrtygkdwdFKPGPFVPPEDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQE 195

                          90       100
                  ....*....|....*....|.
gi 122692531  692 AGAECELAREQRDALEVQVKK 712
Cdd:PRK11448  196 LEAQLEQLQEKAAETSQERKQ 216
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
645-722 7.40e-06

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 47.90  E-value: 7.40e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 122692531 645 AELARLRQELDEANGTIKQWEEswkQAKQACDAWKKE-AEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLHS 722
Cdd:COG1842   51 ANQKRLERQLEELEAEAEKWEE---KARLALEKGREDlAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLES 126
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
644-760 1.50e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531  644 AAELARLRQE---LDEANGTIKQWEESWKQAKQacdawkkEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERL 720
Cdd:COG4913   667 EREIAELEAElerLDASSDDLAALEEQLEELEA-------ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 122692531  721 hsgPDPQALPAFPGLEA-LSLSTLHSLQKRLRAHLE-QVDKA 760
Cdd:COG4913   740 ---EDLARLELRALLEErFAAALGDAVERELRENLEeRIDAL 778
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
644-802 1.72e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.50  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531 644 AAELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLH-- 721
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRer 399

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531 722 ---SGPDPQALPAFPGLEALSLSTLHSLQKRLRAHLEQVDKAVfhmqsvkclkcqEQNRAVLpcqhavlcelcAEGsECP 798
Cdd:PRK02224 400 fgdAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV------------EEAEALL-----------EAG-KCP 455


                 ....*
gi 122692531 799 VC-QP 802
Cdd:PRK02224 456 ECgQP 460
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
645-720 3.43e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531  645 AELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAEC-----------ELAREQRDALEVQVKKL 713
Cdd:COG4913   699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleerfaaalgdAVERELRENLEERIDAL 778


                  ....*..
gi 122692531  714 QEELERL 720
Cdd:COG4913   779 RARLNRA 785
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
645-759 3.48e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 3.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531 645 AELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLHSGP 724
Cdd:COG4372   66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 122692531 725 DPQalpafpglEAlSLSTLHSLQKRLRAHLEQVDK 759
Cdd:COG4372  146 AER--------EE-ELKELEEQLESLQEELAALEQ 171
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 645-722 8.59e-05

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 44.67  E-value: 8.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531  645 AELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGErasaAGAEcELARE---QRDALEVQVKKLQEELERLH 721
Cdd:pfam04012  36 SELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALT----KGNE-ELAREalaEKKSLEKQAEALETQLAQQR 110


                  .
gi 122692531  722 S 722
Cdd:pfam04012 111 S 111
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
646-761 8.72e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 8.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531 646 ELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECEL------------AREQRDALEVQVKKL 713
Cdd:COG4717   96 ELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLeeleerleelreLEEELEELEAELAEL 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 122692531 714 QEELERLHSGPDPQALPAFPGL----EALS--LSTLHSLQKRLRAHLEQVDKAV 761
Cdd:COG4717  176 QEELEELLEQLSLATEEELQDLaeelEELQqrLAELEEELEEAQEELEELEEEL 229
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
768-801 1.28e-04

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 40.05  E-value: 1.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 122692531  768 KCLKCQEQNR--AVLPCQHAVLCELCAE-----GSECPVCQ 801
Cdd:pfam13920   4 LCVICLDRPRnvVLLPCGHLCLCEECAErllrkKKKCPICR 44
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 645-719 1.37e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 42.21  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531  645 AELARLRQELDEANGTIKQWEESWKQAKQA---CDAWKKEAEEAGER----ASAAGAECELAREQRDALEVQVKKLQEEL 717
Cdd:pfam20492  20 EETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERleesAEMEAEEKEQLEAELAEAQEEIARLEEEV 99


                  ..
gi 122692531  718 ER 719
Cdd:pfam20492 100 ER 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 645-793 1.70e-04

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: 45.43  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531   645 AELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLHSgp 724
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS-- 386

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 122692531   725 dpqalpAFPGLEaLSLSTLHSLQKRLRAHLEQVDKAVFHMQSVKCLKCQEQNRAVLPCQHAVLCELCAE 793
Cdd:TIGR02168  387 ------KVAQLE-LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE 448
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
644-761 2.38e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531  644 AAELARLRQELDEANGTIKQWEESWKQAKQACDAWKkeaeeagERASAAGAECELAREQRDALEVQ--VKKLQEELERLH 721
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ-------ERREALQRLAEYSWDEIDVASAEreIAELEAELERLD 681

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 122692531  722 SGPDpqalpafpGLEAL--SLSTLHSLQKRLRAHLEQVDKAV 761
Cdd:COG4913   682 ASSD--------DLAALeeQLEELEAELEELEEELDELKGEI 715
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 644-720 2.77e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.77e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 122692531 644 AAELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERL 720
Cdd:COG1196  245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
646-758 3.35e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531  646 ELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEA-GERASAAGAECELAREQRDALEVQVKKLQEELERLHSGP 724
Cdd:COG4913   289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALL 368

                          90       100       110
                  ....*....|....*....|....*....|....
gi 122692531  725 DPQALPAfpgleALSLSTLHSLQKRLRAHLEQVD 758
Cdd:COG4913   369 AALGLPL-----PASAEEFAALRAEAAALLEALE 397
mRING-HC-C3HC5_MGRN1-like cd16789
Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 ...
 767-800 6.06e-04

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


Pssm-ID: 438443 [Multi-domain]  Cd Length: 42  Bit Score: 38.05  E-value: 6.06e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 122692531 767 VKCLkCQEQNRAVLPCQHAVLCELCAE-----GSECPVC 800
Cdd:cd16789    4 VICL-SDPRDTAVLPCRHLCLCSDCAEvlryqSNKCPIC 41
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
 637-720 1.13e-03

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 41.45  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531  637 AFLSGPGAAelarlrQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEE 716
Cdd:pfam11932   4 LLLASGALA------ATLDQALDLAEKAVAAAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQE 77


                  ....
gi 122692531  717 LERL 720
Cdd:pfam11932  78 IASL 81
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 644-760 1.26e-03

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: 42.35  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531   644 AAELARLRQELDEANGTIKQWEES-------WKQAKQACDAWKKEAE-------EAGERASAAGAECELAREQRDALEVQ 709
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAEleeleaeLEELESRLEELEEQLEtlrskvaQLELQIASLNNEIERLEARLERLEDR 415

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 122692531   710 VKKLQEELERLHSGPDPQALPAFPGLEALSLSTLHSLQKRLRAHLEQVDKA 760
Cdd:TIGR02168  416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
294-320 1.55e-03

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 36.40  E-value: 1.55e-03
                          10        20
                  ....*....|....*....|....*..
gi 122692531  294 YKSTKCNDMQQSGSCPRGPFCAFAHVE 320
Cdd:pfam00642   1 YKTELCRFFLRTGYCKYGDRCKFAHGQ 27
mRING-HC-C3HC5_CGRF1-like cd16649
Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 ...
 769-800 1.70e-03

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


Pssm-ID: 438311 [Multi-domain]  Cd Length: 40  Bit Score: 36.92  E-value: 1.70e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 122692531 769 CLKCQEQNRAV--LPCQHAVLCELCAEGS---ECPVC 800
Cdd:cd16649    3 CVVCLENPASVllLPCRHLCLCEVCAKGLrgkTCPIC 39
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
645-720 1.85e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531 645 AELARLRQELDEANGTIKQWEE---SWKQAKQACDAWKKEAEEAGERASAAGA--------ECELAREQRDALEVQVKKL 713
Cdd:COG4717  139 AELAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEQLSLATEeelqdlaeELEELQQRLAELEEELEEA 218


                 ....*..
gi 122692531 714 QEELERL 720
Cdd:COG4717  219 QEELEEL 225
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 644-720 2.64e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 2.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 122692531 644 AAELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERL 720
Cdd:COG1196  308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 644-721 3.09e-03

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 41.17  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531  644 AAELARLR--QELDEANGTIK---------QWEEswKQAKQACDAWKKEAEE-----AGERASAAGAECELAREQRDALE 707
Cdd:pfam05701  60 AAEAAKAQvlEELESTKRLIEelklnleraQTEE--AQAKQDSELAKLRVEEmeqgiADEASVAAKAQLEVAKARHAAAV 137

                          90
                  ....*....|....
gi 122692531  708 VQVKKLQEELERLH 721
Cdd:pfam05701 138 AELKSVKEELESLR 151
mukB PRK04863
chromosome partition protein MukB;
635-763 3.17e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.10  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531  635 SPAFLSGPgAAELARLRQELDEA-------NGTIKQWEESWKQAKQACDAWKKEAEEAGERASAA-GAECELAREQRDAL 706
Cdd:PRK04863  828 AVAFEADP-EAELRQLNRRRVELeraladhESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETlADRVEEIREQLDEA 906

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 122692531  707 EVQVKKLQ------EELERLHSG--PDPQALPAFPGLEALSLSTLHSLQKRLRAhLEQVDKAVFH 763
Cdd:PRK04863  907 EEAKRFVQqhgnalAQLEPIVSVlqSDPEQFEQLKQDYQQAQQTQRDAKQQAFA-LTEVVQRRAH 970
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 637-721 4.19e-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: 40.13  E-value: 4.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531 637 AFLSGPGAAELAR-LRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQE 715
Cdd:COG4942   11 LALAAAAQADAAAeAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90


                 ....*.
gi 122692531 716 ELERLH 721
Cdd:COG4942   91 EIAELR 96
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
645-720 5.28e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 5.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531 645 AELARLRQELDEANGTIKQW-EESWK------QAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEEL 717
Cdd:COG1340  167 AELKELRKEAEEIHKKIKELaEEAQElheemiELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKEL 246


                 ...
gi 122692531 718 ERL 720
Cdd:COG1340  247 KKL 249
CTH1 COG5063
CCCH-type Zn-finger protein [General function prediction only];
124-318 5.51e-03

CCCH-type Zn-finger protein [General function prediction only];


Pssm-ID: 227395 [Multi-domain]  Cd Length: 351  Bit Score: 40.04  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531 124 YYKTGICIHETDaKGNCTkNGLHCAFAHGPHDLR-SPVYDIRELQAMEALQNGQTTVEGSMEGQSAGAASHAMIEKILSE 202
Cdd:COG5063  112 LYKTEMLRSSTE-IPYCR-YPDKNPFAHSKAISSlAQTHPKYKTESLEVFINPGYVPYSKRCCFISLPLTDINLQPLSQR 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531 203 EPR--WQETAYVLG-NYKTEPC---------------KKPPRLC----RQGYaCPYYHNSKDRRRSPRKH---------- 250
Cdd:COG5063  190 KPKsgKNCTSYTLGkESDAHPHdeliyqkqeqnkplyKTNPELCesftRKGT-CPYWISGVKCQFACRGHglnelkskkk 268

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 122692531 251 --KYRSSPCPNvkhgdeWGDPGKCENGDSCQYCHTRTEQQFHPE----IYKSTKCNDMQQSGSCPRGPFCAFAH 318
Cdd:COG5063  269 kqNFRTEPCIN------WEKSGYCPYGLRCCFKHGDDSDIEMYEeaslGYLDGPCRTRAKGGAFPSGGAVCKSF 336
PCRF pfam03462
PCRF domain; This domain is found in peptide chain release factors.
 635-726 6.21e-03

PCRF domain; This domain is found in peptide chain release factors.


Pssm-ID: 460929 [Multi-domain]  Cd Length: 192  Bit Score: 38.52  E-value: 6.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122692531  635 SPAFLSGPgaAELARLRQELDEANGTIKQWEEsWKQAKQACDAWK---KEAEEAgerasaagaecELAREQRDALEVQVK 711
Cdd:pfam03462  14 DPDVWDDQ--KRAQKLSKEYSELEPIVEAYRE-YKQALEDLEEAKellEDPELA-----------ELAEEELEELEKRLE 79

                          90
                  ....*....|....*
gi 122692531  712 KLQEELERLHSGPDP 726
Cdd:pfam03462  80 ELEEELKLLLLPKDP 94
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 665-719 6.21e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 39.58  E-value: 6.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 122692531  665 EESWKQAKQACDAWKKEAEEAGERASAAGAECELARE-----------QRDALEVQVKKLQEELER 719
Cdd:pfam02841 189 EEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREkqkeeeqmmeaQERSYQEHVKQLIEKMEA 254
mRING-HC-C3HC5_RNF26 cd16788
Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 26 (RNF26) and ...
 768-800 6.83e-03

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


Pssm-ID: 438442 [Multi-domain]  Cd Length: 60  Bit Score: 35.85  E-value: 6.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 122692531 768 KCLKCQEQNRAV--LPCQHAVLCELCAE--------GSECPVC 800
Cdd:cd16788    7 KCVICQDQSKTVliLPCRHMCLCRQCANillqqpvyRRNCPLC 49
mRING-HC-C3HC5_CGRF1 cd16787
Modified RING finger, HC subclass (C3HC5-type), found in cell growth regulator with RING ...
 769-801 9.77e-03

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


Pssm-ID: 438441 [Multi-domain]  Cd Length: 38  Bit Score: 34.65  E-value: 9.77e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 122692531 769 CLKCQEQ--NRAVLPCQHAVLCELCAEG-SECPVCQ 801
Cdd:cd16787    3 CVVCQNApvNRVLLPCRHACVCDECFKRlQRCPMCR 38
 
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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