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Conserved domains on  [gi|7959151|dbj|BAA95970|]
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KIAA1446 protein, partial [Homo sapiens]

Protein Classification

COG4372 family protein( domain architecture ID 11468211)

COG4372 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
60-184 2.27e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.29  E-value: 2.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151   60 QEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNymaLQRINQELEDKLYRMGQhYEE 139
Cdd:COG4372  37 LFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEELES-LQE 108

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 7959151  140 EKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 184
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
60-184 2.27e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.29  E-value: 2.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151   60 QEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNymaLQRINQELEDKLYRMGQhYEE 139
Cdd:COG4372  37 LFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEELES-LQE 108

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 7959151  140 EKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 184
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 58-174 5.22e-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: 46.59  E-value: 5.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151      58 ALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrmgQHY 137
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----EAL 878

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 7959151     138 EEEKRALSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 174
Cdd:TIGR02168  879 LNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 76-175 1.96e-04

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 41.44  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151     76 KLEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSNYMALQRINQELED---KLYRMGQHYEEEKRALSHEIvaln 152
Cdd:pfam20492  14 RLKQYEEETKKAQE----ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEekeRLEESAEMEAEEKEQLEAEL---- 85

                          90       100
                  ....*....|....*....|...
gi 7959151    153 shlLEAKVTIDKLSEDNElyRKD 175
Cdd:pfam20492  86 ---AEAQEEIARLEEEVE--RKE 103
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 74-191 7.48e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153335 [Multi-domain]  Cd Length: 236  Bit Score: 41.52  E-value: 7.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151   74 THKLEKL-ETEFDSTRhylEIELRRAqeeLEKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRALSHEIval 151
Cdd:cd07651  39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 7959151  152 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 191
Cdd:cd07651 110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
59-174 1.01e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151    59 LQEQKGELRKRLSY-----------TTHKLEKLETEF---DSTRHYLEIELRR---AQEELEKVTEKLRRIQSnymALQR 121
Cdd:PRK03918 568 LEEELAELLKELEElgfesveeleeRLKELEPFYNEYlelKDAEKELEREEKElkkLEEELDKAFEELAETEK---RLEE 644

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7959151   122 INQELED--KLYRMGQHYE--EEKRALSHEIVA-------LNSHLLEAKVTIDKLSEDNELYRK 174
Cdd:PRK03918 645 LRKELEEleKKYSEEEYEElrEEYLELSRELAGlraeleeLEKRREEIKKTLEKLKEELEEREK 708
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
60-184 2.27e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.29  E-value: 2.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151   60 QEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNymaLQRINQELEDKLYRMGQhYEE 139
Cdd:COG4372  37 LFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEELES-LQE 108

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 7959151  140 EKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 184
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
58-206 4.75e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 4.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151   58 ALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSnymALQRINQELEDklyrmgqhY 137
Cdd:COG4372  63 QLEEELEQARSELEQLEEELEELNEQLQAAQA----ELAQAQEELESLQEEAEELQE---ELEELQKERQD--------L 127

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7959151  138 EEEKRALSHEIVALNSHLLEAKVTIDKLSEDNElyrkdcNLAAQLLQCSQTYGRV------HKVSELPSDFQERV 206
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLE------SLQEELAALEQELQALseaeaeQALDELLKEANRNA 196
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 58-174 5.22e-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: 46.59  E-value: 5.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151      58 ALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrmgQHY 137
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----EAL 878

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 7959151     138 EEEKRALSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 174
Cdd:TIGR02168  879 LNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 59-170 1.02e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.15  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151   59 LQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSN---------YMALQ-------RI 122
Cdd:COG1579  29 LPAELAELEDELAALEARLEAAKTELED----LEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeYEALQkeieslkRR 104

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 7959151  123 NQELEDKLYR-MGQ--HYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNE 170
Cdd:COG1579 105 ISDLEDEILElMERieELEEELAELEAELAELEAELEEKKAELDEELAELE 155
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 76-175 1.96e-04

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 41.44  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151     76 KLEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSNYMALQRINQELED---KLYRMGQHYEEEKRALSHEIvaln 152
Cdd:pfam20492  14 RLKQYEEETKKAQE----ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEekeRLEESAEMEAEEKEQLEAEL---- 85

                          90       100
                  ....*....|....*....|...
gi 7959151    153 shlLEAKVTIDKLSEDNElyRKD 175
Cdd:pfam20492  86 ---AEAQEEIARLEEEVE--RKE 103
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 59-142 2.03e-04

Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.


Pssm-ID: 461461 [Multi-domain]  Cd Length: 121  Bit Score: 41.23  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151     59 LQEQKGELRKRLSYTTHKLEKLETEFDSTRHyLEIELRRAQEELEKVTEKLRRIQSNYMALQrinQELEDKLYRMGQhyE 138
Cdd:pfam04871  13 LKNENTELKAELQELSKQYNSLEQKESQAKE-LEAEVKKLEEALKKLKAELSEEKQKEKEKQ---SELDDLLLLLGD--L 86


                  ....
gi 7959151    139 EEKR 142
Cdd:pfam04871  87 EEKV 90
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 58-194 2.28e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 2.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151      58 ALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrmGQHY 137
Cdd:TIGR02169  354 KLTEEYAELKEELEDLRAELEEVDKEFAETRD----ELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL---ADLN 426

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 7959151     138 EEEKRALShEIVALNSHLLEAKVTIDKLSEDNELYRKDC-NLAAQLLQCSQTYGRVHK 194
Cdd:TIGR02169  427 AAIAGIEA-KINELEEEKEDKALEIKKQEWKLEQLAADLsKYEQELYDLKEEYDRVEK 483
Tup_N pfam08581
Tup N-terminal; The N-terminal domain of the Tup protein has been shown to interact with the ...
 77-148 2.57e-04

Tup N-terminal; The N-terminal domain of the Tup protein has been shown to interact with the Ssn6 transcriptional co-repressor.


Pssm-ID: 400755 [Multi-domain]  Cd Length: 77  Bit Score: 39.80  E-value: 2.57e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7959151     77 LEKLETEFDS-TRHYLEIELRRaqEELEkvteklRRIQSNYMALQRINQ---ELEDKLYRMGQHYEEEKRALSHEI 148
Cdd:pfam08581   6 LDAIKQEFDNlSQEANSYKAQR--DEYE------HKINQQINELQQIRQtlyELERAHRKIKQQYEEEIARLKAEL 73
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 58-151 4.04e-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: 43.21  E-value: 4.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151   58 ALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYRMGQHY 137
Cdd:COG4942  24 EAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                        90
                ....*....|....
gi 7959151  138 EEEKRALSHEIVAL 151
Cdd:COG4942 100 EAQKEELAELLRAL 113
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
58-183 4.25e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 4.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151    58 ALQEQKGELRKRLSYTTHKLEKLETEFDSTR------------HYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQE 125
Cdd:COG4913  614 ALEAELAELEEELAEAEERLEALEAELDALQerrealqrlaeySWDEIDVASAEREIAELEAELERLDASSDDLAALEEQ 693

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 7959151   126 LEdKLYRMGQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLL 183
Cdd:COG4913  694 LE-ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 74-191 7.48e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153335 [Multi-domain]  Cd Length: 236  Bit Score: 41.52  E-value: 7.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151   74 THKLEKL-ETEFDSTRhylEIELRRAqeeLEKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRALSHEIval 151
Cdd:cd07651  39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 7959151  152 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 191
Cdd:cd07651 110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 59-197 7.70e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 42.64  E-value: 7.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151   59 LQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEI-ELRRAQEELEKVTEKLRRIQSNYMALQR-INQELEDKLYRMGQH 136
Cdd:COG5185 280 LNENANNLIKQFENTKEKIAEYTKSIDIKKATESLeEQLAAAEAEQELEESKRETETGIQNLTAeIEQGQESLTENLEAI 359

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7959151  137 YEEEKRALSHEIVALNSHLLE-AKVTIDKLSEDNELYRKDCNLAAQLL--QCSQTYGRVHKVSE 197
Cdd:COG5185 360 KEEIENIVGEVELSKSSEELDsFKDTIESTKESLDEIPQNQRGYAQEIlaTLEDTLKAADRQIE 423
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
58-175 8.13e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 8.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151   58 ALQEQKGELRKRLSYTTHKLEKLETEFDstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALqrinQELEDKLYRMGQHY 137
Cdd:COG4717  99 ELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEELEERLEEL----RELEEELEELEAEL 172

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 7959151  138 EEEKRALSHEIVALN----SHLLEAKVTIDKLSEDNELYRKD 175
Cdd:COG4717 173 AELQEELEELLEQLSlateEELQDLAEELEELQQRLAELEEE 214
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
59-174 1.01e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151    59 LQEQKGELRKRLSY-----------TTHKLEKLETEF---DSTRHYLEIELRR---AQEELEKVTEKLRRIQSnymALQR 121
Cdd:PRK03918 568 LEEELAELLKELEElgfesveeleeRLKELEPFYNEYlelKDAEKELEREEKElkkLEEELDKAFEELAETEK---RLEE 644

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7959151   122 INQELED--KLYRMGQHYE--EEKRALSHEIVA-------LNSHLLEAKVTIDKLSEDNELYRK 174
Cdd:PRK03918 645 LRKELEEleKKYSEEEYEElrEEYLELSRELAGlraeleeLEKRREEIKKTLEKLKEELEEREK 708
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 58-169 1.39e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 39.92  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151     58 ALQEQKGELRKRLSYTTHKLEKLETEfDSTRhylEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDklyrmgqhy 137
Cdd:pfam08614  68 ELYRSRGELAQRLVDLNEELQELEKK-LRED---ERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQD--------- 134

                          90       100       110
                  ....*....|....*....|....*....|..
gi 7959151    138 eeekralshEIVALNSHLLEAKVTIDKLSEDN 169
Cdd:pfam08614 135 ---------ELVALQLQLNMAEEKLRKLEKEN 157
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 64-188 1.78e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 39.89  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151     64 GELRKRLSYTTHKLEKLETE-----------------FDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQEL 126
Cdd:pfam15619  14 KELQNELAELQSKLEELRKEnrllkrlqkrqekalgkYEGTESELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEK 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7959151    127 EDKLYRMG---QHYEE--------EKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRK--DCNLAAQLLQCSQT 188
Cdd:pfam15619  94 EAELLRLRdqlKRLEKlsedknlaEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKsfRRQLAAEKKKHKEA 168
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
61-174 1.79e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151    61 EQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKlyrmgqhyEEE 140
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELERE--------EKE 620

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 7959151   141 KRALSHEIVALNSHLLEAKVTIDKLSED-NELYRK 174
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKElEELEKK 655
PRK01156 PRK01156
chromosome segregation protein; Provisional
 58-212 3.12e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.66  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151    58 ALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYRMGQHY 137
Cdd:PRK01156 584 TNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID 663

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7959151   138 EEEKR--ALSHEIVALNSHLLEAKVTIDKLSEDneLYRKDcNLAAQLLQcsqtygRVHKVSELPSDFQERVSlHMEK 212
Cdd:PRK01156 664 SIIPDlkEITSRINDIEDNLKKSRKALDDAKAN--RARLE-STIEILRT------RINELSDRINDINETLE-SMKK 730
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
58-174 3.25e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 3.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151    58 ALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEiELRRAQEELEKV---TEKLRRIQSNYMALQRINQELEDKLYRMg 134
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIE-ELKKEIEELEEKvkeLKELKEKAEEYIKLSEFYEEYLDELREI- 312

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 7959151   135 qhyEEEKRALSHEIVALNSHLLEAKvtiDKLSEDNELYRK 174
Cdd:PRK03918 313 ---EKRLSRLEEEINGIEERIKELE---EKEERLEELKKK 346
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 58-170 3.40e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 3.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151      58 ALQEQKGELRKRLSYTthKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrmgQHY 137
Cdd:TIGR02168  217 ELKAELRELELALLVL--RLEELREELEE----LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI----EEL 286

                           90       100       110
                   ....*....|....*....|....*....|...
gi 7959151     138 EEEKRALSHEIVALNSHLLEAKVTIDKLSEDNE 170
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLERQLE 319
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
59-174 4.69e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 4.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151    59 LQEQKGELRKRLSYTTHKLEKLEtefdstrhyleIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYRMGQhYE 138
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEIS-----------SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK-LE 258

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 7959151   139 EEKRALSHEIVALNSHL--LEAKVT-IDKLSEDNELYRK 174
Cdd:PRK03918 259 EKIRELEERIEELKKEIeeLEEKVKeLKELKEKAEEYIK 297
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 59-165 5.38e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.16  E-value: 5.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151      59 LQEqkgELRKRLSYTThKLEKLETEFDSTRHYLEielrraqEELEKVTEKLRRIQSNYMALQRINQELEDKLYRMGQhYE 138
Cdd:pfam01576  477 LQE---ETRQKLNLST-RLRQLEDERNSLQEQLE-------EEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-LE 544

                           90       100
                   ....*....|....*....|....*..
gi 7959151     139 EEKRALSHEIVALNSHLLEAKVTIDKL 165
Cdd:pfam01576  545 EGKKRLQRELEALTQQLEEKAAAYDKL 571
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 58-174 5.96e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 5.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151      58 ALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKL----RRIQSNYMALQRINQELEDKLYRM 133
Cdd:TIGR02169  802 KLEEEVSRIEARLREIEQKLNRLTLE----KEYLEKEIQELQEQRIDLKEQIksieKEIENLNGKKEELEEELEELEAAL 877

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 7959151     134 GQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRK 174
Cdd:TIGR02169  878 RD-LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 59-131 6.59e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 37.56  E-value: 6.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7959151     59 LQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYM-ALQRINQELEDKLY 131
Cdd:pfam03938  24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQqELQKKQQELLQPIQ 97
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 91-169 7.89e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.00  E-value: 7.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151   91 LEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDklyrmgqhyeeekralshEIVALNSH--LLEAKvtIDKLSED 168
Cdd:cd22887   9 LEKRLAELEAELASLEEEIKDLEEELKEKNKANEILND------------------ELIALQIEnnLLEEK--LRKLQEE 68


                .
gi 7959151  169 N 169
Cdd:cd22887  69 N 69
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 58-184 8.57e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 8.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7959151   58 ALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrmgQHY 137
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELARLEQDIARLEERR----REL 314

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 7959151  138 EEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 184
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
 
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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