NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1867162749|ref|NP_001372016|]
View 

brain-enriched guanylate kinase-associated protein isoform 4 [Homo sapiens]

Protein Classification

COG4372 family protein( domain architecture ID 11468211)

COG4372 family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
25-174 2.81e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.98  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  25 LCLGQPRVLQGRLARSSPSIWDSALQEQKgELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQS 104
Cdd:COG4372    13 LSLFGLRPKTGILIAALSEQLRKALFELD-KLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNE 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749 105 NymaLQRINQELEDKLYRMGQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 174
Cdd:COG4372    88 Q---LQAAQAELAQAQEELES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
25-174 2.81e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.98  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  25 LCLGQPRVLQGRLARSSPSIWDSALQEQKgELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQS 104
Cdd:COG4372    13 LSLFGLRPKTGILIAALSEQLRKALFELD-KLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNE 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749 105 NymaLQRINQELEDKLYRMGQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 174
Cdd:COG4372    88 Q---LQAAQAELAQAQEELES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 47-164 2.50e-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: 47.74  E-value: 2.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749   47 SALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrmgQH 126
Cdd:TIGR02168  806 DELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----EA 877

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1867162749  127 YEEEKRALSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 164
Cdd:TIGR02168  878 LLNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 52-165 1.41e-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: 41.83  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  52 QKGELRKRLsytthklEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSNYMALQRINQELED---KLYRMGQHYE 128
Cdd:pfam20492   7 EKQELEERL-------KQYEEETKKAQE----ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEekeRLEESAEMEA 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1867162749 129 EEKRALSHEIvalnshlLEAKVTIDKLSEDNElyRKD 165
Cdd:pfam20492  76 EEKEQLEAEL-------AEAQEEIARLEEEVE--RKE 103
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 64-181 7.34e-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: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  64 THKLEKL-ETEFDSTRhylEIELRRAqeeLEKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRALSHEIval 141
Cdd:cd07651    39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1867162749 142 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 181
Cdd:cd07651   110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
49-164 8.91e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 8.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  49 LQEQKGELRKRLSY-----------TTHKLEKLETEF---DSTRHYLEIELRR---AQEELEKVTEKLRRIQSnymALQR 111
Cdd:PRK03918  568 LEEELAELLKELEElgfesveeleeRLKELEPFYNEYlelKDAEKELEREEKElkkLEEELDKAFEELAETEK---RLEE 644

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1867162749 112 INQELED--KLYRMGQHYE--EEKRALSHEIVA-------LNSHLLEAKVTIDKLSEDNELYRK 164
Cdd:PRK03918  645 LRKELEEleKKYSEEEYEElrEEYLELSRELAGlraeleeLEKRREEIKKTLEKLKEELEEREK 708
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
25-174 2.81e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.98  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  25 LCLGQPRVLQGRLARSSPSIWDSALQEQKgELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQS 104
Cdd:COG4372    13 LSLFGLRPKTGILIAALSEQLRKALFELD-KLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNE 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749 105 NymaLQRINQELEDKLYRMGQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 174
Cdd:COG4372    88 Q---LQAAQAELAQAQEELES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 47-164 2.50e-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: 47.74  E-value: 2.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749   47 SALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrmgQH 126
Cdd:TIGR02168  806 DELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL----EA 877

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1867162749  127 YEEEKRALSHEIVALNSHLLEAKVTIDKLSEDN-ELYRK 164
Cdd:TIGR02168  878 LLNERASLEEALALLRSELEELSEELRELESKRsELRRE 916
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
47-196 3.03e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 3.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  47 SALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSnymALQRINQELEDklyrmgqh 126
Cdd:COG4372    62 EQLEEELEQARSELEQLEEELEELNEQLQAAQA----ELAQAQEELESLQEEAEELQE---ELEELQKERQD-------- 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1867162749 127 YEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNElyrkdcNLAAQLLQCSQTYGRV------HKVSELPSDFQERV 196
Cdd:COG4372   127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLE------SLQEELAALEQELQALseaeaeQALDELLKEANRNA 196
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 49-160 9.90e-05

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: 9.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  49 LQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSN---------YMALQ-------RI 112
Cdd:COG1579    29 LPAELAELEDELAALEARLEAAKTELED----LEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeYEALQkeieslkRR 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1867162749 113 NQELEDKLYR-MGQ--HYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNE 160
Cdd:COG1579   105 ISDLEDEILElMERieELEEELAELEAELAELEAELEEKKAELDEELAELE 155
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 52-165 1.41e-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: 41.83  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  52 QKGELRKRLsytthklEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSNYMALQRINQELED---KLYRMGQHYE 128
Cdd:pfam20492   7 EKQELEERL-------KQYEEETKKAQE----ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEekeRLEESAEMEA 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1867162749 129 EEKRALSHEIvalnshlLEAKVTIDKLSEDNElyRKD 165
Cdd:pfam20492  76 EEKEQLEAEL-------AEAQEEIARLEEEVE--RKE 103
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 47-132 1.85e-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: 41.62  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  47 SALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyLEIELRRAQEELEKVTEKLRRIQSNYMALQrinQELEDKLYRMGQh 126
Cdd:pfam04871  11 SSLKNENTELKAELQELSKQYNSLEQKESQAKE-LEAEVKKLEEALKKLKAELSEEKQKEKEKQ---SELDDLLLLLGD- 85


                  ....*.
gi 1867162749 127 yEEEKR 132
Cdd:pfam04871  86 -LEEKV 90
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 48-184 1.88e-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: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749   48 ALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrmGQHY 127
Cdd:TIGR02169  354 KLTEEYAELKEELEDLRAELEEVDKEFAETRD----ELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL---ADLN 426

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1867162749  128 EEEKRALShEIVALNSHLLEAKVTIDK-------LSEDNELYRKdcnlaaQLLQCSQTYGRVHK 184
Cdd:TIGR02169  427 AAIAGIEA-KINELEEEKEDKALEIKKqewkleqLAADLSKYEQ------ELYDLKEEYDRVEK 483
Tup_N pfam08581
Tup N-terminal; The N-terminal domain of the Tup protein has been shown to interact with the ...
 67-138 2.60e-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: 2.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1867162749  67 LEKLETEFDS-TRHYLEIELRRaqEELEkvteklRRIQSNYMALQRINQ---ELEDKLYRMGQHYEEEKRALSHEI 138
Cdd:pfam08581   6 LDAIKQEFDNlSQEANSYKAQR--DEYE------HKINQQINELQQIRQtlyELERAHRKIKQQYEEEIARLKAEL 73
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-173 2.89e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749   48 ALQEQKGELRKRLSYTTHKLEKLETEFDSTR------------HYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQE 115
Cdd:COG4913    614 ALEAELAELEEELAEAEERLEALEAELDALQerrealqrlaeySWDEIDVASAEREIAELEAELERLDASSDDLAALEEQ 693

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1867162749  116 LEdKLYRMGQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLL 173
Cdd:COG4913    694 LE-ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 47-141 2.92e-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: 43.60  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  47 SALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYRMGQH 126
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90
                  ....*....|....*
gi 1867162749 127 YEEEKRALSHEIVAL 141
Cdd:COG4942    99 LEAQKEELAELLRAL 113
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 47-178 3.26e-04

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: 42.20  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  47 SALQEQKGELRKRLSYTTHKLEKLETE-----------------FDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMAL 109
Cdd:pfam15619   7 SARLHKIKELQNELAELQSKLEELRKEnrllkrlqkrqekalgkYEGTESELPQLIARHNEEVRVLRERLRRLQEKERDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749 110 QRINQELEDKLYRMG---QHYEE--------EKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRK--DCNLAAQLLQCS 176
Cdd:pfam15619  87 ERKLKEKEAELLRLRdqlKRLEKlsedknlaEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKsfRRQLAAEKKKHK 166


                  ..
gi 1867162749 177 QT 178
Cdd:pfam15619 167 EA 168
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 38-164 4.27e-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: 43.52  E-value: 4.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749   38 ARSSPSIWD------SALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKL----RRIQSNYM 107
Cdd:TIGR02169  786 ARLSHSRIPeiqaelSKLEEEVSRIEARLREIEQKLNRLTLE----KEYLEKEIQELQEQRIDLKEQIksieKEIENLNG 861

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1867162749  108 ALQRINQELEDKLYRMGQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRK 164
Cdd:TIGR02169  862 KKEELEEELEELEAALRD-LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
47-165 6.16e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 6.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  47 SALQEQKGELRKRLSYTTHKLEKLETEFDstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALqrinQELEDKLYRMGQH 126
Cdd:COG4717    98 EELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEELEERLEEL----RELEEELEELEAE 171

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1867162749 127 YEEEKRALSHEIVALN----SHLLEAKVTIDKLSEDNELYRKD 165
Cdd:COG4717   172 LAELQEELEELLEQLSlateEELQDLAEELEELQQRLAELEEE 214
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 64-181 7.34e-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: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  64 THKLEKL-ETEFDSTRhylEIELRRAqeeLEKV-TEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRALSHEIval 141
Cdd:cd07651    39 AKRLEKLsRKSLGGSE---EGGLKNS---LDTLrLETESMAKSHLKFAKQIRQDLEEKLAAFASSYTQKRKKIQSHM--- 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1867162749 142 nSHLLEAKVTIDK-LSEDNELYRKDCN-LAAQLLQCSQTYGR 181
Cdd:cd07651   110 -EKLLKKKQDQEKyLEKAREKYEADCSkINSYTLQSQLTWGK 150
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 49-187 7.55e-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: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  49 LQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEI-ELRRAQEELEKVTEKLRRIQSNYMALQR-INQELEDKLYRMGQH 126
Cdd:COG5185   280 LNENANNLIKQFENTKEKIAEYTKSIDIKKATESLeEQLAAAEAEQELEESKRETETGIQNLTAeIEQGQESLTENLEAI 359

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1867162749 127 YEEEKRALSHEIVALNSHLLE-AKVTIDKLSEDNELYRKDCNLAAQLL--QCSQTYGRVHKVSE 187
Cdd:COG5185   360 KEEIENIVGEVELSKSSEELDsFKDTIESTKESLDEIPQNQRGYAQEIlaTLEDTLKAADRQIE 423
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
49-164 8.91e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 8.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  49 LQEQKGELRKRLSY-----------TTHKLEKLETEF---DSTRHYLEIELRR---AQEELEKVTEKLRRIQSnymALQR 111
Cdd:PRK03918  568 LEEELAELLKELEElgfesveeleeRLKELEPFYNEYlelKDAEKELEREEKElkkLEEELDKAFEELAETEK---RLEE 644

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1867162749 112 INQELED--KLYRMGQHYE--EEKRALSHEIVA-------LNSHLLEAKVTIDKLSEDNELYRK 164
Cdd:PRK03918  645 LRKELEEleKKYSEEEYEElrEEYLELSRELAGlraeleeLEKRREEIKKTLEKLKEELEEREK 708
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
48-164 1.08e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  48 ALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEiELRRAQEELEKVTEKLRRIQ---SNYMALQRINQELEDKLYRMg 124
Cdd:PRK03918  235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELKekaEEYIKLSEFYEEYLDELREI- 312

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1867162749 125 qhyEEEKRALSHEIVALNSHLLEAKvtiDKLSEDNELYRK 164
Cdd:PRK03918  313 ---EKRLSRLEEEINGIEERIKELE---EKEERLEELKKK 346
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
51-164 1.46e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  51 EQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKlyrmgqhyEEE 130
Cdd:PRK03918  549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELERE--------EKE 620

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1867162749 131 KRALSHEIVALNSHLLEAKVTIDKLSED-NELYRK 164
Cdd:PRK03918  621 LKKLEEELDKAFEELAETEKRLEELRKElEELEKK 655
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 47-159 1.50e-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: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  47 SALQEQKGELRKRLSYTTHKLEKLETEfDSTRhylEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDklyrmgqh 126
Cdd:pfam08614  67 AELYRSRGELAQRLVDLNEELQELEKK-LRED---ERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQD-------- 134

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1867162749 127 yeeekralshEIVALNSHLLEAKVTIDKLSEDN 159
Cdd:pfam08614 135 ----------ELVALQLQLNMAEEKLRKLEKEN 157
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 48-160 2.84e-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: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749   48 ALQEQKGELRKRLSYTthKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrmgQHY 127
Cdd:TIGR02168  217 ELKAELRELELALLVL--RLEELREELEE----LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI----EEL 286

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1867162749  128 EEEKRALSHEIVALNSHLLEAKVTIDKLSEDNE 160
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLERQLE 319
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 46-131 2.95e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  46 DSALQEQKgELRKRLSyttHKLEKLETEFDSTRHYLEIE----LRRAQEELEKVTEKLRRIQSNYMALQRiNQELEDKLY 121
Cdd:PRK00409  540 EALLKEAE-KLKEELE---EKKEKLQEEEDKLLEEAEKEaqqaIKEAKKEADEIIKELRQLQKGGYASVK-AHELIEARK 614

                          90
                  ....*....|
gi 1867162749 122 RMGQHYEEEK 131
Cdd:PRK00409  615 RLNKANEKKE 624
PRK01156 PRK01156
chromosome segregation protein; Provisional
 48-202 3.06e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.66  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  48 ALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYRMGQHY 127
Cdd:PRK01156  584 TNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID 663

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1867162749 128 EEEKR--ALSHEIVALNSHLLEAKVTIDKLSEDneLYRKDcNLAAQLLQcsqtygRVHKVSELPSDFQERVSlHMEK 202
Cdd:PRK01156  664 SIIPDlkEITSRINDIEDNLKKSRKALDDAKAN--RARLE-STIEILRT------RINELSDRINDINETLE-SMKK 730
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
49-164 3.84e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  49 LQEQKGELRKRLSYTTHKLEKLEtefdstrhyleIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYRMGQhYE 128
Cdd:PRK03918  191 IEELIKEKEKELEEVLREINEIS-----------SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK-LE 258

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1867162749 129 EEKRALSHEIVALNSHL--LEAKVT-IDKLSEDNELYRK 164
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 ...
 49-155 5.79e-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: 39.77  E-value: 5.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749   49 LQEqkgELRKRLSYTThKLEKLETEFDSTRHYLEielrraqEELEKVTEKLRRIQSNYMALQRINQELEDKLYRMGQhYE 128
Cdd:pfam01576  477 LQE---ETRQKLNLST-RLRQLEDERNSLQEQLE-------EEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-LE 544

                           90       100
                   ....*....|....*....|....*..
gi 1867162749  129 EEKRALSHEIVALNSHLLEAKVTIDKL 155
Cdd:pfam01576  545 EGKKRLQRELEALTQQLEEKAAAYDKL 571
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
33-173 6.14e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  33 LQGRLARSSPSIWDSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyLEIELRRAQEELEKVTEKLRRiqsnymALQRI 112
Cdd:COG4717   114 LREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQEELEE------LLEQL 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1867162749 113 NQELEDKLYRMGQHYEE---EKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLL 173
Cdd:COG4717   187 SLATEEELQDLAEELEElqqRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 49-121 6.48e-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: 6.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1867162749  49 LQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYM-ALQRINQELEDKLY 121
Cdd:pfam03938  24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQqELQKKQQELLQPIQ 97
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 48-174 6.79e-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: 6.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  48 ALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrmgQHY 127
Cdd:COG1196   243 ELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELARLEQDIARLEERR----REL 314

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1867162749 128 EEEKRALSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQ 174
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 81-159 7.76e-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: 7.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749  81 LEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDklyrmgqhyeeekralshEIVALNSH--LLEAKvtIDKLSED 158
Cdd:cd22887     9 LEKRLAELEAELASLEEEIKDLEEELKEKNKANEILND------------------ELIALQIEnnLLEEK--LRKLQEE 68


                  .
gi 1867162749 159 N 159
Cdd:cd22887    69 N 69
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 48-153 8.95e-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: 39.28  E-value: 8.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867162749   48 ALQEQKGELRkrLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYRMGqhy 127
Cdd:TIGR02169  215 ALLKEKREYE--GYELLKEKEALERQ----KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG--- 285

                           90       100
                   ....*....|....*....|....*.
gi 1867162749  128 EEEKRALSHEIVALNSHLLEAKVTID 153
Cdd:TIGR02169  286 EEEQLRVKEKIGELEAEIASLERSIA 311
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH