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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907081388 464 QSVKCLKCQEQTRAVLPCQHAVLCELCAEGSECPVCQPSRAH 505
Cdd:cd16771     1 QSVKCLKCQELKRVTLPCQHALLCETCATSEECPICHPHRPH 42

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907081388 464 QSVKCLKCQEQTRAVLPCQHAVLCELCAEGSECPVCQPSRAH 505
Cdd:cd16771     1 QSVKCLKCQELKRVTLPCQHALLCETCATSEECPICHPHRPH 42

type I restriction enzyme EcoKI subunit R; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081388  319 SIWEH--------FASGSFSPGTSPAFLSGPGAAELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASA 390
Cdd:PRK11448   116 AVWFHrtygkdwdFKPGPFVPPEDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQE 195

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081388  391 AGAECELAREQRDALElrvkklQEELERLHtvpeAQTLPAApdlEALSLS---TLYSIQKQLR 450
Cdd:PRK11448   196 LEAQLEQLQEKAAETS------QERKQKRK----EITDQAA---KRLELSeeeTRILIDQQLR 245

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081388 344 AELARLRQELDEANGTIKQWEESWKQAKQA---CDAWKKEAEEAGER----ASAAGAECELAREQRDALELRVKKLQEEL 416
Cdd:pfam20492  20 EETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERleesAEMEAEEKEQLEAELAEAQEEIARLEEEV 99

                  ..
gi 1907081388 417 ER 418
Cdd:pfam20492 100 ER 101

polarized growth protein Scy;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081388  338 LSGPGAAELARLRQELDEANGTI-KQWEESWKQAKQACDAWKKEAEEAGE--RASAAGAECELAREQRDALELRVKKLQE 414
Cdd:NF041483   496 LRSTATAESERVRTEAIERATTLrRQAEETLERTRAEAERLRAEAEEQAEevRAAAERAARELREETERAIAARQAEAAE 575

                           90
                   ....*....|....*..
gi 1907081388  415 ELERLHTVPEaQTLPAA 431
Cdd:NF041483   576 ELTRLHTEAE-ERLTAA 591

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907081388 464 QSVKCLKCQEQTRAVLPCQHAVLCELCAEGSECPVCQPSRAH 505
Cdd:cd16771     1 QSVKCLKCQELKRVTLPCQHALLCETCATSEECPICHPHRPH 42

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.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907081388 467 KCLKCQEQTRAVL--PCQHAVLCELCAEGS-ECPVCQ 500
Cdd:cd16772     2 KCIVCQERDRSIVlqPCQHYVLCEHCAASKpECPYCK 38

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081388 344 AELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALELRVKKLQEELERL 419
Cdd:COG4372    45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120

type I restriction enzyme EcoKI subunit R; Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081388  319 SIWEH--------FASGSFSPGTSPAFLSGPGAAELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASA 390
Cdd:PRK11448   116 AVWFHrtygkdwdFKPGPFVPPEDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQE 195

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081388  391 AGAECELAREQRDALElrvkklQEELERLHtvpeAQTLPAApdlEALSLS---TLYSIQKQLR 450
Cdd:PRK11448   196 LEAQLEQLQEKAAETS------QERKQKRK----EITDQAA---KRLELSeeeTRILIDQQLR 245

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081388 344 AELARLRQELDEANGTIKQWEESWKQAKQA---CDAWKKEAEEAGER----ASAAGAECELAREQRDALELRVKKLQEEL 416
Cdd:pfam20492  20 EETKKAQEELEESEETAEELEEERRQAEEEaerLEQKRQEAEEEKERleesAEMEAEEKEQLEAELAEAQEEIARLEEEV 99

                  ..
gi 1907081388 417 ER 418
Cdd:pfam20492 100 ER 101

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.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907081388 468 CLKCQEQTRAV--LPCQHAVLCELCAEGS---ECPVC 499
Cdd:cd16649     3 CVVCLENPASVllLPCRHLCLCEVCAKGLrgkTCPIC 39

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]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081388  344 AELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALELRVKKLQEELERLHtvp 423
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR--- 385

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081388  424 eaqtlpaapDLEALSLSTLYSIQKQ---LRVHLEQVDKAVFHMQSVKCLKCQEQTRAVLPCQHAVLCELCAE 492
Cdd:TIGR02168  386 ---------SKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE 448

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081388 344 AELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGErasaAGAEcELAREqrdALElRVKKLQEELERLHTVp 423
Cdd:pfam04012  36 SELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALT----KGNE-ELARE---ALA-EKKSLEKQAEALETQ- 105

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907081388 424 eaqtlpaapdlealslstlysiQKQLRVHLEQVDKAV 460
Cdd:pfam04012 106 ----------------------LAQQRSAVEQLRKQL 120

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081388  343 AAELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAR--EQRDALEL---RVKKLQEELE 417
Cdd:COG4913    616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAEleAELERLDAssdDLAALEEQLE 695

                   ...
gi 1907081388  418 RLH 420
Cdd:COG4913    696 ELE 698

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.

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907081388 466 VKCLkCQEQTRAVLPCQHAVLCELCAE-----GSECPVC 499
Cdd:cd16789     4 VICL-SDPRDTAVLPCRHLCLCSDCAEvlryqSNKCPIC 41

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]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081388  343 AAELARLRQELDEANGTIKQWEES-------WKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALELRVKKLQEE 415
Cdd:TIGR02168  336 AEELAELEEKLEELKEELESLEAEleeleaeLEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1907081388  416 LERLHT-VPEAQTLPAAPDLEALS--LSTLYSIQKQLRVHLEQV 456
Cdd:TIGR02168  416 RERLQQeIEELLKKLEEAELKELQaeLEELEEELEELQEELERL 459

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081388 345 ELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECEL------------AREQRDALELRVKKL 412
Cdd:COG4717    96 ELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLeeleerleelreLEEELEELEAELAEL 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907081388 413 QEELERLHTVPEAQTL----PAAPDLEALS--LSTLYSIQKQLRVHLEQVDKAV 460
Cdd:COG4717   176 QEELEELLEQLSLATEeelqDLAEELEELQqrLAELEEELEEAQEELEELEEEL 229

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081388 343 AAELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALELRVKKLQEELERL 419
Cdd:COG1196   308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081388 344 AELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALELRVKKLQEELERLHTvp 423
Cdd:COG4372    94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ-- 171

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907081388 424 EAQTLPAAPDLEALS--LSTLYSIQKQLRVHLEQVDKAVF 461
Cdd:COG4372   172 ELQALSEAEAEQALDelLKEANRNAEKEEELAEAEKLIES 211

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081388 336 AFLSGPGAAELAR-LRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALELRVKKLQE 414
Cdd:COG4942    11 LALAAAAQADAAAeAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90

                          90
                  ....*....|..
gi 1907081388 415 ELERLHTVPEAQ 426
Cdd:COG4942    91 EIAELRAELEAQ 102

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.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907081388 468 CLKCQEQ--TRAVLPCQHAVLCELCAEG-SECPVCQ 500
Cdd:cd16787     3 CVVCQNApvNRVLLPCRHACVCDECFKRlQRCPMCR 38

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081388  336 AFLSGPgAAELARLRQ-------ELDEANGTIKQWEESWKQAKQACDAWKK--------EAEEAGERASAAGAECELARE 400
Cdd:COG3096    829 AFAPDP-EAELAALRQrrselerELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanllADETLADRLEELREELDAAQE 907

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081388  401 QRDALELRVKKLqEELErlhtvPEAQTLPAAP-DLEALSLSTLYSIQKQlrvhlEQVDKAVFHMQSV 466
Cdd:COG3096    908 AQAFIQQHGKAL-AQLE-----PLVAVLQSDPeQFEQLQADYLQAKEQQ-----RRLKQQIFALSEV 963

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1907081388 468 CLKCQEQ--TRAVLPCQHAVLCELCA------EGSECPVCQPSRAHALQ 508
Cdd:cd16518     3 CVVCFESevVAALVPCGHNLFCMECAnricekSDPECPVCHTPVTQAIR 51

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081388 344 AELAR----LRQELD--EANGTIKQW---EESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALELRVKKLQE 414
Cdd:COG1196   209 AEKAEryreLKEELKelEAELLLLKLrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288

                  ....*
gi 1907081388 415 ELERL 419
Cdd:COG1196   289 EEYEL 293

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081388 344 AELARLRQELDEANGTIKQWEEswkQAKQACDAwkKEAEEAGERASAAGAECELA------REQRDALELRVKKLQEELE 417
Cdd:pfam09486  22 AELEAARAALAQAEAALAAAQA---QAEQARDR--VRAHEERLDDLTTGGSPFSAadylacRAYRDVLEGRVGAAEAALA 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907081388 418 RLHtvpeaQTLPAAPDLEALSLSTLYSIQKQLRVHLEQVDKA 459
Cdd:pfam09486  97 AAR-----QALDAAEDAVAATRRKIARNDAQLDVCRERIARL 133

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081388 348 RLRQELDEangTIKQWEEswkQAKQAcdawKKEAEEAGERASAAGAECELAREQRDALELRVKKLQEELERL 419
Cdd:pfam20492   6 REKQELEE---RLKQYEE---ETKKA----QEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERL 67

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081388 343 AAELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEAGERASAAGAECELAREQRDALELRVKKLQEELERLHTV 422
Cdd:COG1196   671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750

                          90
                  ....*....|....*
gi 1907081388 423 PEAQTLPAAPDLEAL 437
Cdd:COG1196   751 EALEELPEPPDLEEL 765

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081388 343 AAELARLRQELDEANGTIKQWEESWKQAKQACDAWKKEAEEA-GERASAAGAECELAREQRDALELRVKKLQEELERLHT 421
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAeAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907081388 422 VPEAQTLPAAPDLEALSLSTLYSIQKQLRVHLEQVDKA 459
Cdd:COG1196   395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432