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Conserved domains on  [gi|767996283|ref|XP_011523703|]
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RING finger protein unkempt homolog isoform X6 [Homo sapiens]

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, ...
 475-516 1.32e-19

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: 81.79  E-value: 1.32e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767996283 475 QSVKCLKCQEQKRAVLPCQHAALCELCAEGSECPICQPGRAH 516
Cdd:cd16771    1 QSVKCLKCQELKRVTLPCQHALLCETCATSEECPICHPHRPH 42
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
353-432 4.13e-07

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: 53.00  E-value: 4.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  353 GAAELARLRQELDEANSTIKQWEESWKQAKQAC-----------DAWKKEAEEAGERASAAGAECELAREQRDALEVQVK 421
Cdd:COG4913   336 GGDRLEQLEREIERLERELEERERRRARLEALLaalglplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415

                          90
                  ....*....|.
gi 767996283  422 KLQEELERLHA 432
Cdd:COG4913   416 DLRRELRELEA 426
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
4-30 9.72e-05

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


:

Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 39.48  E-value: 9.72e-05
                          10        20
                  ....*....|....*....|....*..
gi 767996283    4 YKSTKCNDMQQSGSCPRGPFCAFAHVE 30
Cdd:pfam00642   1 YKTELCRFFLRTGYCKYGDRCKFAHGQ 27
 
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, ...
 475-516 1.32e-19

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: 81.79  E-value: 1.32e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767996283 475 QSVKCLKCQEQKRAVLPCQHAALCELCAEGSECPICQPGRAH 516
Cdd:cd16771    1 QSVKCLKCQELKRVTLPCQHALLCETCATSEECPICHPHRPH 42
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
353-432 4.13e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 4.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  353 GAAELARLRQELDEANSTIKQWEESWKQAKQAC-----------DAWKKEAEEAGERASAAGAECELAREQRDALEVQVK 421
Cdd:COG4913   336 GGDRLEQLEREIERLERELEERERRRARLEALLaalglplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415

                          90
                  ....*....|.
gi 767996283  422 KLQEELERLHA 432
Cdd:COG4913   416 DLRRELRELEA 426
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 330-422 2.38e-06

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 50.34  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  330 SIWEH--------FASGSFSPGTSPAFLSGPGAAELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASA 401
Cdd:PRK11448  116 AVWFHrtygkdwdFKPGPFVPPEDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQE 195

                          90       100
                  ....*....|....*....|.
gi 767996283  402 AGAECELAREQRDALEVQVKK 422
Cdd:PRK11448  196 LEAQLEQLQEKAAETSQERKQ 216
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
478-511 3.33e-06

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 44.29  E-value: 3.33e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 767996283  478 KCLKCQEQKR--AVLPCQHAALCELCAE-----GSECPICQ 511
Cdd:pfam13920   4 LCVICLDRPRnvVLLPCGHLCLCEECAErllrkKKKCPICR 44
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 355-503 3.25e-05

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: 46.97  E-value: 3.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283   355 AELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLhagp 434
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL---- 384

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767996283   435 epqalpafSDLEALSLSTLYSLQKQ---LRAHLEQVDKAVFHMQSVKCLKCQEQKRAVLPCQHAALCELCAE 503
Cdd:TIGR02168  385 --------RSKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE 448
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 355-477 6.63e-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: 44.29  E-value: 6.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  355 AELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGErasaAGAEcELARE---QRDALEVQVKKLQEELERLH 431
Cdd:pfam04012  36 SELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALT----KGNE-ELAREalaEKKSLEKQAEALETQLAQQR 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767996283  432 AGPEpQALPAFSDLEAlSLSTLYSlQKQLRAHLEQVDKAVFHMQSV 477
Cdd:pfam04012 111 SAVE-QLRKQLAALET-KIQQLKA-KKNLLKARLKAAKAQEAVQTS 153
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
4-30 9.72e-05

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


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 39.48  E-value: 9.72e-05
                          10        20
                  ....*....|....*....|....*..
gi 767996283    4 YKSTKCNDMQQSGSCPRGPFCAFAHVE 30
Cdd:pfam00642   1 YKTELCRFFLRTGYCKYGDRCKFAHGQ 27
growth_prot_Scy NF041483
polarized growth protein Scy;
349-435 5.30e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.89  E-value: 5.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  349 LSGPGAAELARLRQELDEANSTI-KQWEESWKQAKQACDAWKKEAEEAGE--RASAAGAECELAREQRDALEVQVKKLQE 425
Cdd:NF041483  496 LRSTATAESERVRTEAIERATTLrRQAEETLERTRAEAERLRAEAEEQAEevRAAAERAARELREETERAIAARQAEAAE 575

                          90
                  ....*....|
gi 767996283  426 ELERLHAGPE 435
Cdd:NF041483  576 ELTRLHTEAE 585
ZnF_C3H1 smart00356
zinc finger;
4-30 9.57e-03

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 33.76  E-value: 9.57e-03
                           10        20
                   ....*....|....*....|....*..
gi 767996283     4 YKSTKCNDmQQSGSCPRGPFCAFAHVE 30
Cdd:smart00356   2 YKTELCKF-FKRGYCPRGDRCKFAHPL 27
 
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, ...
 475-516 1.32e-19

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: 81.79  E-value: 1.32e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767996283 475 QSVKCLKCQEQKRAVLPCQHAALCELCAEGSECPICQPGRAH 516
Cdd:cd16771    1 QSVKCLKCQELKRVTLPCQHALLCETCATSEECPICHPHRPH 42
RING-HC_UNK-like cd16614
RING finger, HC subclass, found in RING finger protein unkempt (UNK), unkempt-like (UNKL), and ...
 477-511 6.33e-11

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: 57.18  E-value: 6.33e-11
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 767996283 477 VKCLKCQEQKR--AVLPCQHAALCELCAEGS-ECPICQ 511
Cdd:cd16614    1 KKCMKCEERNRsvAVLPCQHYVLCEQCAETAtECPYCH 38
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
353-432 4.13e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 4.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  353 GAAELARLRQELDEANSTIKQWEESWKQAKQAC-----------DAWKKEAEEAGERASAAGAECELAREQRDALEVQVK 421
Cdd:COG4913   336 GGDRLEQLEREIERLERELEERERRRARLEALLaalglplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415

                          90
                  ....*....|.
gi 767996283  422 KLQEELERLHA 432
Cdd:COG4913   416 DLRRELRELEA 426
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
355-471 5.06e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.83  E-value: 5.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283 355 AELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLHAgp 434
Cdd:COG4372   45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK-- 122

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767996283 435 EPQAlpafsdlealslstLYSLQKQLRAHLEQVDKAV 471
Cdd:COG4372  123 ERQD--------------LEQQRKQLEAQIAELQSEI 145
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
354-470 1.01e-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: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  354 AAELARLRQE---LDEANSTIKQWEESWKQAKQacdawkkEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERL 430
Cdd:COG4913   667 EREIAELEAElerLDASSDDLAALEEQLEELEA-------ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767996283  431 hagPEPQALPAFSDLEA-LSLSTLYSLQKQLRAHLE-QVDKA 470
Cdd:COG4913   740 ---EDLARLELRALLEErFAAALGDAVERELRENLEeRIDAL 778
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 330-422 2.38e-06

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 50.34  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  330 SIWEH--------FASGSFSPGTSPAFLSGPGAAELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASA 401
Cdd:PRK11448  116 AVWFHrtygkdwdFKPGPFVPPEDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQE 195

                          90       100
                  ....*....|....*....|.
gi 767996283  402 AGAECELAREQRDALEVQVKK 422
Cdd:PRK11448  196 LEAQLEQLQEKAAETSQERKQ 216
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
355-432 2.41e-06

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 48.67  E-value: 2.41e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767996283 355 AELARLRQELDEANSTIKQWEEswkQAKQACDAWKKE-AEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLHA 432
Cdd:COG1842   51 ANQKRLERQLEELEAEAEKWEE---KARLALEKGREDlAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLES 126
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
354-482 2.83e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.04  E-value: 2.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283 354 AAELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLH-- 431
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRer 399

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767996283 432 ---AGPEPQALPAFSDLEALSLSTLYSLQKQLRAHLEQVDKAVFHMQSV----KCLKC 482
Cdd:PRK02224 400 fgdAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALleagKCPEC 457
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
356-486 2.89e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 2.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283 356 ELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECEL------------AREQRDALEVQVKKL 423
Cdd:COG4717   96 ELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLeeleerleelreLEEELEELEAELAEL 175

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767996283 424 QEELERLHAGPEPQALPAFSDL----EALS--LSTLYSLQKQLRAHLEQVDKAVFHMQSVKCLKCQEQK 486
Cdd:COG4717  176 QEELEELLEQLSLATEEELQDLaeelEELQqrLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
355-470 3.14e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.52  E-value: 3.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283 355 AELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLHAGP 434
Cdd:COG4372   66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767996283 435 EPQAlpafSDLEALSlSTLYSLQKQLRAhLEQVDKA 470
Cdd:COG4372  146 AERE----EELKELE-EQLESLQEELAA-LEQELQA 175
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
478-511 3.33e-06

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 44.29  E-value: 3.33e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 767996283  478 KCLKCQEQKR--AVLPCQHAALCELCAE-----GSECPICQ 511
Cdd:pfam13920   4 LCVICLDRPRnvVLLPCGHLCLCEECAErllrkKKKCPICR 44
RING-HC_UNKL cd16772
RING finger, HC subclass, found in RING finger protein unkempt-like (UNKL) and similar ...
 478-511 5.79e-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: 43.24  E-value: 5.79e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767996283 478 KCLKCQEQKRAVL--PCQHAALCELCAEGS-ECPICQ 511
Cdd:cd16772    2 KCIVCQERDRSIVlqPCQHYVLCEHCAASKpECPYCK 38
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
355-469 1.81e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283 355 AELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLHAGP 434
Cdd:COG4372   59 EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI 138

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767996283 435 EpQALPAFSDLEAlSLSTLYSLQKQLRAHLEQVDK 469
Cdd:COG4372  139 A-ELQSEIAEREE-ELKELEEQLESLQEELAALEQ 171
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
354-470 1.82e-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: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  354 AAELARLRQELDEANSTIKQWEESWKQAKQACDAWKkeaeeagERASAAGAECELAREQRDALEVQ--VKKLQEELERLH 431
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ-------ERREALQRLAEYSWDEIDVASAEreIAELEAELERLD 681

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767996283  432 AGPepqalpafSDLEALSlSTLYSLQKQLRAHLEQVDKA 470
Cdd:COG4913   682 ASS--------DDLAALE-EQLEELEAELEELEEELDEL 711
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
354-470 1.87e-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: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  354 AAELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAR--EQRDALE---VQVKKLQEELE 428
Cdd:COG4913   616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAEleAELERLDassDDLAALEEQLE 695

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767996283  429 RLHAgpEPQALpaFSDLEALSlSTLYSLQKQLRAHLEQVDKA 470
Cdd:COG4913   696 ELEA--ELEEL--EEELDELK-GEIGRLEKELEQAEEELDEL 732
mRING-HC-C3HC5_CGRF1-like cd16649
Modified RING finger, HC subclass (C3HC5-type), found in RING finger proteins, RNF26, RNF197 ...
 479-510 2.76e-05

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: 41.15  E-value: 2.76e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767996283 479 CLKCQEQKRAV--LPCQHAALCELCAEGS---ECPIC 510
Cdd:cd16649    3 CVVCLENPASVllLPCRHLCLCEVCAKGLrgkTCPIC 39
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 355-503 3.25e-05

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: 46.97  E-value: 3.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283   355 AELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLhagp 434
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL---- 384

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767996283   435 epqalpafSDLEALSLSTLYSLQKQ---LRAHLEQVDKAVFHMQSVKCLKCQEQKRAVLPCQHAALCELCAE 503
Cdd:TIGR02168  385 --------RSKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE 448
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 354-432 5.55e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 5.55e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767996283 354 AAELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLHA 432
Cdd:COG1196  245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 355-477 6.63e-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: 44.29  E-value: 6.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  355 AELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGErasaAGAEcELARE---QRDALEVQVKKLQEELERLH 431
Cdd:pfam04012  36 SELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALT----KGNE-ELAREalaEKKSLEKQAEALETQLAQQR 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767996283  432 AGPEpQALPAFSDLEAlSLSTLYSlQKQLRAHLEQVDKAVFHMQSV 477
Cdd:pfam04012 111 SAVE-QLRKQLAALET-KIQQLKA-KKNLLKARLKAAKAQEAVQTS 153
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
355-470 6.71e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 6.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  355 AELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEA-GERASAAGAECELAREQRDALEVQVKKLQEELERLHAg 433
Cdd:COG4913   295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGL- 373

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767996283  434 PEPQALPAFSDLEALSLSTLYSLQKQLRAHLEQVDKA 470
Cdd:COG4913   374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEA 410
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 355-429 6.77e-05

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: 42.60  E-value: 6.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  355 AELARLRQELDEANSTIKQWEESWKQAKQA---CDAWKKEAEEAGER----ASAAGAECELAREQRDALEVQVKKLQEEL 427
Cdd:pfam20492  20 EETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERleesAEMEAEEKEQLEAELAEAQEEIARLEEEV 99


                  ..
gi 767996283  428 ER 429
Cdd:pfam20492 100 ER 101
mRING-HC-C3HC5_MGRN1-like cd16789
Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 ...
 477-510 7.23e-05

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: 39.98  E-value: 7.23e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767996283 477 VKCLkCQEQKRAVLPCQHAALCELCAE-----GSECPIC 510
Cdd:cd16789    4 VICL-SDPRDTAVLPCRHLCLCSDCAEvlryqSNKCPIC 41
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
4-30 9.72e-05

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


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 39.48  E-value: 9.72e-05
                          10        20
                  ....*....|....*....|....*..
gi 767996283    4 YKSTKCNDMQQSGSCPRGPFCAFAHVE 30
Cdd:pfam00642   1 YKTELCRFFLRTGYCKYGDRCKFAHGQ 27
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
 347-430 3.71e-04

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: 42.22  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  347 AFLSGPGAAelarlrQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEE 426
Cdd:pfam11932   4 LLLASGALA------ATLDQALDLAEKAVAAAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQE 77


                  ....
gi 767996283  427 LERL 430
Cdd:pfam11932  78 IASL 81
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
355-432 4.55e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 4.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283 355 AELARLRQELDEANSTIKQWEE---SWKQAKQACDAWKKEAEEAGERASAAGA--------ECELAREQRDALEVQVKKL 423
Cdd:COG4717  139 AELAELPERLEELEERLEELREleeELEELEAELAELQEELEELLEQLSLATEeelqdlaeELEELQQRLAELEEELEEA 218


                 ....*....
gi 767996283 424 QEELERLHA 432
Cdd:COG4717  219 QEELEELEE 227
growth_prot_Scy NF041483
polarized growth protein Scy;
349-435 5.30e-04

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 42.89  E-value: 5.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  349 LSGPGAAELARLRQELDEANSTI-KQWEESWKQAKQACDAWKKEAEEAGE--RASAAGAECELAREQRDALEVQVKKLQE 425
Cdd:NF041483  496 LRSTATAESERVRTEAIERATTLrRQAEETLERTRAEAERLRAEAEEQAEevRAAAERAARELREETERAIAARQAEAAE 575

                          90
                  ....*....|
gi 767996283  426 ELERLHAGPE 435
Cdd:NF041483  576 ELTRLHTEAE 585
mRING-HC-C3HC5_RNF26 cd16788
Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 26 (RNF26) and ...
 478-510 6.29e-04

Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 26 (RNF26) and similar proteins; RNF26 is an E3 ubiquitin ligase that temporally regulates virus-triggered type I interferon induction by increasing the stability of Mediator of IRF3 activation, MITA, also known as STING, through K11-linked polyubiquitination of MITA after viral infection, and promoting 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: 38.17  E-value: 6.29e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 767996283 478 KCLKCQEQKRAV--LPCQHAALCELCAE--------GSECPIC 510
Cdd:cd16788    7 KCVICQDQSKTVliLPCRHMCLCRQCANillqqpvyRRNCPLC 49
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 354-470 6.57e-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: 42.74  E-value: 6.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283   354 AAELARLRQELDEANSTIKQWEESWKQAKqacdawKKEAEEAGERASAAgAECELAREQRDALEVQVKKLQEELERLHAG 433
Cdd:TIGR02168  357 EAELEELEAELEELESRLEELEEQLETLR------SKVAQLELQIASLN-NEIERLEARLERLEDRRERLQQEIEELLKK 429

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 767996283   434 PEPQALPAFSDLEALSLSTLYSLQKQLRAHLEQVDKA 470
Cdd:TIGR02168  430 LEEAELKELQAELEELEEELEELQEELERLEEALEEL 466
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 347-432 7.92e-04

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: 41.67  E-value: 7.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283 347 AFLSGPGAAELAR-LRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQE 425
Cdd:COG4942   11 LALAAAAQADAAAeAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90


                 ....*..
gi 767996283 426 ELERLHA 432
Cdd:COG4942   91 EIAELRA 97
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 354-467 8.56e-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: 42.35  E-value: 8.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283   354 AAELARLRQELDEA-------NSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEE 426
Cdd:TIGR02168  336 AEELAELEEKLEELkeeleslEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 767996283   427 LERLHA---GPEPQALPAFSDLEALSLSTLYSLQKQLRAHLEQV 467
Cdd:TIGR02168  416 RERLQQeieELLKKLEEAELKELQAELEELEEELEELQEELERL 459
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 354-467 1.24e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.86  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  354 AAELARLRQELDEANSTIKQWEESWKQAKQACDA------WKKEAEEAGERASAAGAECelaREQRDALEVQVKKLQEEL 427
Cdd:COG3096   518 RAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAaeeleeLLAELEAQLEELEEQAAEA---VEQRSELRQQLEQLRARI 594

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767996283  428 ERLHAgPEPQALPAFSDLEAL---SLSTLYSLQkQLRAHLEQV 467
Cdd:COG3096   595 KELAA-RAPAWLAAQDALERLreqSGEALADSQ-EVTAAMQQL 635
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 354-430 1.24e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767996283 354 AAELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERL 430
Cdd:COG1196  308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
355-467 1.26e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283 355 AELARLRQELDEANSTIKQWEESWKQAKQACDAWK-------------KEAEEAGERASAAGAECElaREqRDALEVQVK 421
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETRDEADevleeheerreelETLEAEIEDLRETIAETE--RE-REELAEEVR 282

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767996283 422 KLQEELERLhaGPEPQALPAFSDLEALSLSTLYSLQKQLRAHLEQV 467
Cdd:PRK02224 283 DLRERLEEL--EEERDDLLAEAGLDDADAEAVEARREELEDRDEEL 326
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
355-432 1.74e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  355 AELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAEC------------------ELAREQRDAL 416
Cdd:COG4913   699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleerfaaalgdaverelrENLEERIDAL 778

                          90
                  ....*....|....*.
gi 767996283  417 EVQVKKLQEELERLHA 432
Cdd:COG4913   779 RARLNRAEEELERAMR 794
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
355-430 1.86e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 40.28  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283 355 AELARLRQELDEANSTIKQW-EESWK------QAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEEL 427
Cdd:COG1340  167 AELKELRKEAEEIHKKIKELaEEAQElheemiELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKEL 246


                 ...
gi 767996283 428 ERL 430
Cdd:COG1340  247 KKL 249
mRING-HC-C3HC5_CGRF1 cd16787
Modified RING finger, HC subclass (C3HC5-type), found in cell growth regulator with RING ...
 479-511 2.08e-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: 35.81  E-value: 2.08e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767996283 479 CLKCQEQK--RAVLPCQHAALCELCAEG-SECPICQ 511
Cdd:cd16787    3 CVVCQNAPvnRVLLPCRHACVCDECFKRlQRCPMCR 38
RING-HC_XBAT35-like cd23129
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and ...
 479-516 2.13e-03

RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and similar proteins; XBAT35, also known as ankyrin repeat domain and RING finger-containing protein XBAT35, or RING-type E3 ubiquitin transferase XBAT35, has no E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro. It contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438491 [Multi-domain]  Cd Length: 54  Bit Score: 36.47  E-value: 2.13e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767996283 479 CLKCQEQKR-AVL-PCQHAALCELCA-----EGSECPICqpgRAH 516
Cdd:cd23129    5 CVVCMDAPRdAVCvPCGHVAGCMSCLkalmqSSPLCPIC---RAP 46
HrpB7 pfam09486
Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes ...
 355-470 2.53e-03

Bacterial type III secretion protein (HrpB7); This entry represents proteins encoded by genes which are found in type III secretion operons in a narrow range of species including Xanthomonas, Burkholderia and Ralstonia.


Pssm-ID: 370523 [Multi-domain]  Cd Length: 157  Bit Score: 38.58  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  355 AELARLRQELDEANSTIKQWEEswkQAKQACDAwkKEAEEAGERASAAGAECELA------REQRDALEVQVKKLQEELE 428
Cdd:pfam09486  22 AELEAARAALAQAEAALAAAQA---QAEQARDR--VRAHEERLDDLTTGGSPFSAadylacRAYRDVLEGRVGAAEAALA 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767996283  429 RLHagpepQALPAFSDLEALSLSTLYSLQKQL---RAHLEQVDKA 470
Cdd:pfam09486  97 AAR-----QALDAAEDAVAATRRKIARNDAQLdvcRERIARLRRA 136
mukB PRK04863
chromosome partition protein MukB;
357-475 2.66e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283  357 LARLRQELDEANSTikqwEESWKQAKQACDAW-----------KKEA------EEAGERASAAGAECELAREQRDALEVQ 419
Cdd:PRK04863  309 LVEMARELAELNEA----ESDLEQDYQAASDHlnlvqtalrqqEKIEryqadlEELEERLEEQNEVVEEADEQQEENEAR 384

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767996283  420 VKKLQEELERL----------------HAGPEPQALPAF------SDLEALSLSTLYSLQKQLRAHLEQVDKAVFHMQ 475
Cdd:PRK04863  385 AEAAEEEVDELksqladyqqaldvqqtRAIQYQQAVQALerakqlCGLPDLTADNAEDWLEEFQAKEQEATEELLSLE 462
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 355-470 3.21e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283 355 AELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLHAGp 434
Cdd:COG1196  267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE- 345

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767996283 435 EPQALPAFSDLEALSLSTLYSLQKQLRAHLEQVDKA 470
Cdd:COG1196  346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 375-429 4.34e-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: 39.19  E-value: 4.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767996283  375 EESWKQAKQACDAWKKEAEEAGERASAAGAECELARE-----------QRDALEVQVKKLQEELER 429
Cdd:pfam02841 189 EEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREkqkeeeqmmeaQERSYQEHVKQLIEKMEA 254
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 355-432 4.49e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767996283 355 AELAR----LRQELD--EANSTIKQW---EESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQE 425
Cdd:COG1196  209 AEKAEryreLKEELKelEAELLLLKLrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288


                 ....*..
gi 767996283 426 ELERLHA 432
Cdd:COG1196  289 EEYELLA 295
RING-HC_MIBs cd16519
RING finger, HC subclass, found in mind bomb MIB1, MIB2, and similar proteins; MIBs are large, ...
 479-511 4.91e-03

RING finger, HC subclass, found in mind bomb MIB1, MIB2, and similar proteins; MIBs are large, multi-domain E3 ubiquitin-protein ligases that promote ubiquitination of the cytoplasmic tails of Notch ligands. They are also responsible for TBK1 K63-linked ubiquitination and activation, promoting interferon production and controlling antiviral immunity. Moreover, MIBs selectively control responses to cytosolic RNA and regulate type I interferon transcription. Both MIB1 and MIB2 have similar domain architectures, which consist of two Mib-Herc2 domains flanking a ZZ zinc finger, a REP region including two tandem Mib repeats, an ANK region that spans ankyrin repeats, and a RNG region, where MIB1 and MIB2 contain three and two C3HC4-type RING-HC fingers, respectively. This model corresponds to the first RING-HC finger of MIB1 and MIB2, as well as the second RING-HC finger of MIB1.


Pssm-ID: 438182  Cd Length: 38  Bit Score: 34.76  E-value: 4.91e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767996283 479 CLKCQEQKRAVL--PCQHAALCELCA-EGSECPICQ 511
Cdd:cd16519    3 CRVCSDKKALVLfqPCGHVVACEECSlRMKKCLQCK 38
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 354-432 5.76e-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: 38.98  E-value: 5.76e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767996283 354 AAELARLRQELDEANSTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERLHA 432
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 359-430 7.23e-03

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: 36.43  E-value: 7.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767996283  359 RLRQELDEansTIKQWEEswkQAKQAcdawKKEAEEAGERASAAGAECELAREQRDALEVQVKKLQEELERL 430
Cdd:pfam20492   6 REKQELEE---RLKQYEE---ETKKA----QEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERL 67
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 355-430 7.30e-03

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 36.85  E-value: 7.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767996283  355 AELARLRQELDEANSTIKQWEESWKQAKQacdAWKKEAEEAGERasaagaecelareqRDALEVQVKKLQEELERL 430
Cdd:pfam07926  71 AEIAELKAEAESAKAELEESEESWEEQKK---ELEKELSELEKR--------------IEDLNEQNKLLHDQLESL 129
ZnF_C3H1 smart00356
zinc finger;
4-30 9.57e-03

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 33.76  E-value: 9.57e-03
                           10        20
                   ....*....|....*....|....*..
gi 767996283     4 YKSTKCNDmQQSGSCPRGPFCAFAHVE 30
Cdd:smart00356   2 YKTELCKF-FKRGYCPRGDRCKFAHPL 27
 
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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