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Conserved domains on  [gi|1867157819|ref|NP_001372022|]
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brain-enriched guanylate kinase-associated protein isoform 10 [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];
21-144 1.34e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.75  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNymaLQRINQELEDKLYRM 100
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEEL 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1867157819 101 GQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSE--DNLPSDFQER 144
Cdd:COG4372   104 ES-LQEEAEELQEELEELQKERQDLEQQRKQLEAqiAELQSEIAER 148
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
21-144 1.34e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.75  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNymaLQRINQELEDKLYRM 100
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEEL 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1867157819 101 GQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSE--DNLPSDFQER 144
Cdd:COG4372   104 ES-LQEEAEELQEELEELQKERQDLEQQRKQLEAqiAELQSEIAER 148
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 21-136 7.80e-06

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: 48.90  E-value: 7.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819   21 EKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrm 100
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--- 875

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1867157819  101 gQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDN 136
Cdd:TIGR02168  876 -EALLNERASLEEALALLRSELEELSEELRELESKR 910
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 21-109 4.88e-05

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: 43.16  E-value: 4.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyLEIELRRAQEELEKVTEKLRRIQSNYMALQrinQELEDKLYRM 100
Cdd:pfam04871   8 SEASSLKNENTELKAELQELSKQYNSLEQKESQAKE-LEAEVKKLEEALKKLKAELSEEKQKEKEKQ---SELDDLLLLL 83


                  ....*....
gi 1867157819 101 GQhyEEEKR 109
Cdd:pfam04871  84 GD--LEEKV 90
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
34-135 1.51e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  34 RKRLSYTTHKLEKLETEFDSTRHYLEielrRAQEELEKVTEKLRRIQSNYmalqriNQELEDKLYRMGQHYEEEKRALSH 113
Cdd:PRK03918  611 EKELEREEKELKKLEEELDKAFEELA----ETEKRLEELRKELEELEKKY------SEEEYEELREEYLELSRELAGLRA 680

                          90       100
                  ....*....|....*....|..
gi 1867157819 114 EIVALNSHLLEAKVTIDKLSED 135
Cdd:PRK03918  681 ELEELEKRREEIKKTLEKLKEE 702
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 20-153 4.22e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 39.62  E-value: 4.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819   20 MEKLSALQEQKGELRKRLSYTTHK---LEKLETEFDStrhYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDK 96
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEElrqLKQLEDELED---CDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESK 240

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1867157819   97 LyrmgqhyeEEKRALSHEIVALNSHLLEAKVTIDKLSEDNLPSdFQERVSLHMEKHG 153
Cdd:smart00787 241 I--------EDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEK-LKEQLKLLQSLTG 288
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 58-136 7.10e-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: 7.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  58 LEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDklyrmgqhyeeekralshEIVALNSH--LLEAKvtIDKLSED 135
Cdd:cd22887     9 LEKRLAELEAELASLEEEIKDLEEELKEKNKANEILND------------------ELIALQIEnnLLEEK--LRKLQEE 68


                  .
gi 1867157819 136 N 136
Cdd:cd22887    69 N 69
 
Name Accession Description Interval E-value
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
21-144 1.34e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.75  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNymaLQRINQELEDKLYRM 100
Cdd:COG4372    31 EQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQ---LQAAQAELAQAQEEL 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1867157819 101 GQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSE--DNLPSDFQER 144
Cdd:COG4372   104 ES-LQEEAEELQEELEELQKERQDLEQQRKQLEAqiAELQSEIAER 148
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
21-146 4.46e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.21  E-value: 4.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEI---ELRRAQEELEKVTEKLRRIQSNYMALQRINQELE--- 94
Cdd:COG4372    59 EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQaqeELESLQEEAEELQEELEELQKERQDLEQQRKQLEaqi 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1867157819  95 DKLYRMGQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDNLPSDFQERVS 146
Cdd:COG4372   139 AELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 21-136 7.80e-06

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: 48.90  E-value: 7.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819   21 EKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrm 100
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL--- 875

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1867157819  101 gQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSEDN 136
Cdd:TIGR02168  876 -EALLNERASLEEALALLRSELEELSEELRELESKR 910
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 14-118 9.37e-06

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: 48.22  E-value: 9.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  14 AASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQEL 93
Cdd:COG4942    13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAEL 88

                          90       100
                  ....*....|....*....|....*
gi 1867157819  94 EDKLYRMGQHYEEEKRALSHEIVAL 118
Cdd:COG4942    89 EKEIAELRAELEAQKEELAELLRAL 113
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 15-135 1.60e-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: 46.46  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  15 ASAADMEKLSALQE----------QKGELRKRLSYTTHKLEKLETEFDSTR---HYLEIELRRAQEELEKVTEKLRRIQS 81
Cdd:COG1579     1 AMPEDLRALLDLQEldseldrlehRLKELPAELAELEDELAALEARLEAAKtelEDLEKEIKRLELEIEEVEARIKKYEE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1867157819  82 N---------YMALQ-------RINQELEDKLYR-MGQ--HYEEEKRALSHEIVALNSHLLEAKVTIDKLSED 135
Cdd:COG1579    81 QlgnvrnnkeYEALQkeieslkRRISDLEDEILElMERieELEEELAELEAELAELEAELEEKKAELDEELAE 153
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
21-134 3.79e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 3.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819   21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTR------------HYLEIELRRAQEELEKVTEKLRRIQSNYMALQR 88
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAELDALQerrealqrlaeySWDEIDVASAEREIAELEAELERLDASSDDLAA 689

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1867157819   89 INQELEdKLYRMGQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSE 134
Cdd:COG4913    690 LEEQLE-ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
Uso1_p115_C pfam04871
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ...
 21-109 4.88e-05

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: 43.16  E-value: 4.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyLEIELRRAQEELEKVTEKLRRIQSNYMALQrinQELEDKLYRM 100
Cdd:pfam04871   8 SEASSLKNENTELKAELQELSKQYNSLEQKESQAKE-LEAEVKKLEEALKKLKAELSEEKQKEKEKQ---SELDDLLLLL 83


                  ....*....
gi 1867157819 101 GQhyEEEKR 109
Cdd:pfam04871  84 GD--LEEKV 90
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
21-135 5.92e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 5.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALqrinQELEDKLYRM 100
Cdd:COG4717    95 EELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEELEERLEEL----RELEEELEEL 168

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1867157819 101 GQHYEEEKRALSHeivALNSHLLEAKVTIDKLSED 135
Cdd:COG4717   169 EAELAELQEELEE---LLEQLSLATEEELQDLAEE 200
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
14-138 7.47e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 7.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  14 AASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEF-----DSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQR 88
Cdd:COG4717   381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELeelleALDEEELEEELEELEEELEELEEELEELREELAELEA 460

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1867157819  89 INQELE-----DKLYRMGQHYEEEKRALSHEIVALN--SHLLEAkvTIDKLSEDNLP 138
Cdd:COG4717   461 ELEQLEedgelAELLQELEELKAELRELAEEWAALKlaLELLEE--AREEYREERLP 515
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 23-152 8.79e-05

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: 43.74  E-value: 8.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  23 LSALQEQKGELRKRLSYTTHKLEKLETE-----------------FDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMA 85
Cdd:pfam15619   6 LSARLHKIKELQNELAELQSKLEELRKEnrllkrlqkrqekalgkYEGTESELPQLIARHNEEVRVLRERLRRLQEKERD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  86 LQRINQELEDKLYRMG---QHYEE--------EKRALSHEIVALNSHLLEAKVTIDKLSE--DNLPSDFQERVSLHMEKH 152
Cdd:pfam15619  86 LERKLKEKEAELLRLRdqlKRLEKlsedknlaEREELQKKLEQLEAKLEDKDEKIQDLERklELENKSFRRQLAAEKKKH 165
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
34-135 1.51e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  34 RKRLSYTTHKLEKLETEFDSTRHYLEielrRAQEELEKVTEKLRRIQSNYmalqriNQELEDKLYRMGQHYEEEKRALSH 113
Cdd:PRK03918  611 EKELEREEKELKKLEEELDKAFEELA----ETEKRLEELRKELEELEKKY------SEEEYEELREEYLELSRELAGLRA 680

                          90       100
                  ....*....|....*....|..
gi 1867157819 114 EIVALNSHLLEAKVTIDKLSED 135
Cdd:PRK03918  681 ELEELEKRREEIKKTLEKLKEE 702
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 21-136 1.77e-04

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: 42.61  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEfDSTRhylEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDklyrm 100
Cdd:pfam08614  64 EELAELYRSRGELAQRLVDLNEELQELEKK-LRED---ERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQD----- 134

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1867157819 101 gqhyeeekralshEIVALNSHLLEAKVTIDKLSEDN 136
Cdd:pfam08614 135 -------------ELVALQLQLNMAEEKLRKLEKEN 157
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
21-134 2.38e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEiELRRAQEELEKVTEKLRRIQ---SNYMALQRINQELEDKL 97
Cdd:PRK03918  231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE-ELKKEIEELEEKVKELKELKekaEEYIKLSEFYEEYLDEL 309

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1867157819  98 YRMGQ---HYEEEKRALSHEIVALNSHLLEAKVTIDKLSE 134
Cdd:PRK03918  310 REIEKrlsRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
Tup_N pfam08581
Tup N-terminal; The N-terminal domain of the Tup protein has been shown to interact with the ...
 44-115 2.58e-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: 2.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1867157819  44 LEKLETEFDS-TRHYLEIELRRaqEELEkvteklRRIQSNYMALQRINQ---ELEDKLYRMGQHYEEEKRALSHEI 115
Cdd:pfam08581   6 LDAIKQEFDNlSQEANSYKAQR--DEYE------HKINQQINELQQIRQtlyELERAHRKIKQQYEEEIARLKAEL 73
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
15-146 3.58e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  15 ASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyLEIELRRAQEELEKVTEKLRRiqsnymALQRINQELE 94
Cdd:COG4717   119 EKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE-LEEELEELEAELAELQEELEE------LLEQLSLATE 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1867157819  95 DKLYRMGQHYEE---EKRALSHEIVALNSHLLEAKVTIDKLSEDNLPSDFQERVS 146
Cdd:COG4717   192 EELQDLAEELEElqqRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 43-120 5.27e-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: 39.90  E-value: 5.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  43 KLEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSNYMALQRINQELED---KLYRMGQHYEEEKRALSHEIVALN 119
Cdd:pfam20492  14 RLKQYEEETKKAQE----ELEESEETAEELEEERRQAEEEAERLEQKRQEAEEekeRLEESAEMEAEEKEQLEAELAEAQ 89


                  .
gi 1867157819 120 S 120
Cdd:pfam20492  90 E 90
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 15-135 5.59e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 5.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819   15 ASAAdmEKLSALQEQKGELRKRLSYTthKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELE 94
Cdd:TIGR02168  209 AEKA--ERYKELKAELRELELALLVL--RLEELREELEE----LQEELKEAEEELEELTAELQELEEKLEELRLEVSELE 280

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1867157819   95 DK-----------------LYRMGQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSED 135
Cdd:TIGR02168  281 EEieelqkelyalaneisrLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 18-145 6.86e-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: 42.75  E-value: 6.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819   18 ADMEKLSALQEQKGELRkrLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKL 97
Cdd:TIGR02169  208 EKAERYQALLKEKREYE--GYELLKEKEALERQ----KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI 281

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1867157819   98 YRMGqhyEEEKRALSHEIVALNSHLLEAKVTIDkLSEDNLpSDFQERV 145
Cdd:TIGR02169  282 KDLG---EEEQLRVKEKIGELEAEIASLERSIA-EKEREL-EDAEERL 324
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
28-151 1.17e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  28 EQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYRMgQHYEEE 107
Cdd:PRK03918  549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKEL-KKLEEE 627

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1867157819 108 KRALSHEIVALNSHLLEAKVTIDKLSEDNLPSDFQERVSLHMEK 151
Cdd:PRK03918  628 LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLEL 671
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
20-132 1.51e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  20 MEKLSALQEQKGELRKRLSYTTHKLEKLEtefdsTRHYLEIELRRAQEELEKVTEKLrriqSNYmALQRINQELEdKLYR 99
Cdd:PRK03918  330 IKELEEKEERLEELKKKLKELEKRLEELE-----ERHELYEEAKAKKEELERLKKRL----TGL-TPEKLEKELE-ELEK 398

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1867157819 100 MGQHYEEEKRALSHEIVALNSHLLEAKVTIDKL 132
Cdd:PRK03918  399 AKEEIEEEISKITARIGELKKEIKELKKAIEEL 431
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 22-134 1.52e-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: 41.59  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819   22 KLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSNY-----------MALQRIN 90
Cdd:TIGR02169  351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD----ELKDYREKLEKLKREINELKRELdrlqeelqrlsEELADLN 426

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1867157819   91 QELEDKLYRMGQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSE 134
Cdd:TIGR02169  427 AAIAGIEAKINE-LEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 21-137 1.58e-03

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: 41.48  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEI-ELRRAQEELEKVTEKLRRIQSNYMALQR-INQELEDKLY 98
Cdd:COG5185   275 ESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLeEQLAAAEAEQELEESKRETETGIQNLTAeIEQGQESLTE 354

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1867157819  99 RMGQHYEEEKRALSHEIVALNSHLLE-AKVTIDKLSEDNL 137
Cdd:COG5185   355 NLEAIKEEIENIVGEVELSKSSEELDsFKDTIESTKESLD 394
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
20-134 1.79e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  20 MEKLSALQEQKGELRKRLSytthKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYR 99
Cdd:PRK03918  213 SSELPELREELEKLEKEVK----ELEELKEEIEE----LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE 284

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1867157819 100 MG--QHYEEEKRALSHEIVALNSHLLEAKVTIDKLSE 134
Cdd:PRK03918  285 LKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEE 321
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 21-135 2.08e-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: 41.21  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819   21 EKLSALQEQKGELRKRLSYTTHKLEKLETEfdstRHYLEIELRRAQEELEKVTEKL----RRIQSNYMALQRINQELEDK 96
Cdd:TIGR02169  798 AELSKLEEEVSRIEARLREIEQKLNRLTLE----KEYLEKEIQELQEQRIDLKEQIksieKEIENLNGKKEELEEELEEL 873

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1867157819   97 LYRMGQhYEEEKRALSHEIVALNSHLLEAKVTIDKLSED 135
Cdd:TIGR02169  874 EAALRD-LESRLGDLKKERDELEAQLRELERKIEELEAQ 911
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 21-135 2.14e-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: 41.21  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819   21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLeiELRRAQEELEkVTEKLRRIQSNYMALQRINQELEDkLYRM 100
Cdd:TIGR02169  177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ--ALLKEKREYE-GYELLKEKEALERQKEAIERQLAS-LEEE 252

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1867157819  101 GQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSED 135
Cdd:TIGR02169  253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE 287
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 21-135 2.99e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLyrm 100
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELEELRLELEE----LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL--- 318

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1867157819 101 gQHYEEEKRALSHEIVALNSHLLEAKVTIDKLSED 135
Cdd:COG1196   319 -EELEEELAELEEELEELEEELEELEEELEEAEEE 352
PRK01156 PRK01156
chromosome segregation protein; Provisional
 14-148 3.39e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.27  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  14 AASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQEL 93
Cdd:PRK01156  573 ALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKI 652

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1867157819  94 EDKLYRMGQHYEEEKRalsheIVALNSHLLEAKVTIDKLSE--DNLPSDFQERVSLH 148
Cdd:PRK01156  653 DNYKKQIAEIDSIIPD-----LKEITSRINDIEDNLKKSRKalDDAKANRARLESTI 704
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 21-135 3.56e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.39  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEiELRRAQEELEKVTEKLRR----IQSNymaLQRINQELEDK 96
Cdd:TIGR04523 124 VELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN-DLKKQKEELENELNLLEKeklnIQKN---IDKIKNKLLKL 199

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1867157819  97 LYRMG--QHYEEEKRALSHEIVALNSHLLEAKVTIDKLSED 135
Cdd:TIGR04523 200 ELLLSnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE 240
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
21-150 3.87e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  21 EKLSALQEQKGELRK---------RLSYTTHKLEKLETEFDStrHYLEiELRRAQEELEKVTEKLRRIQSNymaLQRINQ 91
Cdd:PRK03918  473 EKERKLRKELRELEKvlkkeseliKLKELAEQLKELEEKLKK--YNLE-ELEKKAEEYEKLKEKLIKLKGE---IKSLKK 546

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1867157819  92 ELEDKlyrmgQHYEEEKRALSHEIVALNSHLLEAKVTIDKL---SEDNLPSDFQERVSLHME 150
Cdd:PRK03918  547 ELEKL-----EELKKKLAELEKKLDELEEELAELLKELEELgfeSVEELEERLKELEPFYNE 603
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 20-153 4.22e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 39.62  E-value: 4.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819   20 MEKLSALQEQKGELRKRLSYTTHK---LEKLETEFDStrhYLEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDK 96
Cdd:smart00787 164 MKELELLNSIKPKLRDRKDALEEElrqLKQLEDELED---CDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESK 240

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1867157819   97 LyrmgqhyeEEKRALSHEIVALNSHLLEAKVTIDKLSEDNLPSdFQERVSLHMEKHG 153
Cdd:smart00787 241 I--------EDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEK-LKEQLKLLQSLTG 288
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 17-108 4.27e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 4.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  17 AADMEKLsaLQEQKgELRKRLSyttHKLEKLETEFDSTRHYLEIE----LRRAQEELEKVTEKLRRIQSNYMALQRiNQE 92
Cdd:PRK00409  536 AEEAEAL--LKEAE-KLKEELE---EKKEKLQEEEDKLLEEAEKEaqqaIKEAKKEADEIIKELRQLQKGGYASVK-AHE 608

                          90
                  ....*....|....*.
gi 1867157819  93 LEDKLYRMGQHYEEEK 108
Cdd:PRK00409  609 LIEARKRLNKANEKKE 624
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
21-94 4.52e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 4.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1867157819  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTR-HYLEIELRRAQEELEKVTEKLRRIQSNYMALQR----INQELE 94
Cdd:PRK02224  613 EKREALAELNDERRERLAEKRERKRELEAEFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAeigaVENELE 691
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 21-114 5.55e-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: 39.67  E-value: 5.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819   21 EKLSALQEQKGEL-------RKRLSYTTHKLEKLETEFDStrhyLEIELRRAQEE------LEKVTEKLRRIQSNYMALQ 87
Cdd:TIGR02169  896 AQLRELERKIEELeaqiekkRKRLSELKAKLEALEEELSE----IEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRALE 971

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1867157819   88 RIN----QELEDKLYRMGQhYEEEKRALSHE 114
Cdd:TIGR02169  972 PVNmlaiQEYEEVLKRLDE-LKEKRAKLEEE 1001
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 14-110 5.89e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  14 AASAADMEKLSALQEQKGEL---RKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYMALQRIN 90
Cdd:COG4942   143 YLAPARREQAEELRADLAELaalRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222

                          90       100
                  ....*....|....*....|
gi 1867157819  91 QELEDKLYRMGQHYEEEKRA 110
Cdd:COG4942   223 EELEALIARLEAEAAAAAER 242
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 26-98 5.89e-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: 5.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1867157819  26 LQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKLRRIQSNYM-ALQRINQELEDKLY 98
Cdd:pfam03938  24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQqELQKKQQELLQPIQ 97
FlgN pfam05130
FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar ...
 16-91 6.26e-03

FlgN protein; This family includes the FlgN protein and export chaperone involved in flagellar synthesis.


Pssm-ID: 428323 [Multi-domain]  Cd Length: 140  Bit Score: 37.34  E-value: 6.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1867157819  16 SAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEI-ELRRAQEELEKVTEKLRRIQSNYMALQRINQ 91
Cdd:pfam05130  29 KAGDIEALEELTEEKQELLQKLAQLEKERRELLAELGLSPEEATLsELLAKEEEDPELRELWQELLELLERLKELNE 105
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 26-132 6.31e-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: 6.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819   26 LQEqkgELRKRLSYTThKLEKLETEFDSTRHYLEielrraqEELEKVTEKLRRIQSNYMALQRINQELEDKLYRMGQhYE 105
Cdd:pfam01576  477 LQE---ETRQKLNLST-RLRQLEDERNSLQEQLE-------EEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA-LE 544

                           90       100
                   ....*....|....*....|....*..
gi 1867157819  106 EEKRALSHEIVALNSHLLEAKVTIDKL 132
Cdd:pfam01576  545 EGKKRLQRELEALTQQLEEKAAAYDKL 571
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
21-126 6.70e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 6.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  21 EKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEiELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDKLYRM 100
Cdd:PRK03918  293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK 371

                          90       100
                  ....*....|....*....|....*.
gi 1867157819 101 GQHYEEEKRALSHEIVALNSHLLEAK 126
Cdd:PRK03918  372 EELERLKKRLTGLTPEKLEKELEELE 397
Wtap pfam17098
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ...
 20-76 6.72e-03

WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.


Pssm-ID: 465345 [Multi-domain]  Cd Length: 155  Bit Score: 37.66  E-value: 6.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1867157819  20 MEKLSALQEQKGELRKRLSytTHKLEKLETEFDSTRHYLEiELRRAQEELEKVTEKL 76
Cdd:pfam17098  91 MAKCRLLQQENEELGRQLS--EGRIAKLEIELALQKKVVE-ELKKSLEELDEFLIEL 144
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 20-76 6.89e-03

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: 38.37  E-value: 6.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1867157819  20 MEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELEKVTEKL 76
Cdd:COG1579   116 MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 58-136 7.10e-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: 7.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819  58 LEIELRRAQEELEKVTEKLRRIQSNYMALQRINQELEDklyrmgqhyeeekralshEIVALNSH--LLEAKvtIDKLSED 135
Cdd:cd22887     9 LEKRLAELEAELASLEEEIKDLEEELKEKNKANEILND------------------ELIALQIEnnLLEEK--LRKLQEE 68


                  .
gi 1867157819 136 N 136
Cdd:cd22887    69 N 69
mukB PRK04863
chromosome partition protein MukB;
16-114 8.84e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 8.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867157819   16 SAADMEKLSALQEQkgeLRKRLsytthklEKLETEFDSTRHyleiELRRAQEELEKVTEKLRRIQSNYMALQRINQELED 95
Cdd:PRK04863   976 AAEMLAKNSDLNEK---LRQRL-------EQAEQERTRARE----QLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQ 1041

                           90       100
                   ....*....|....*....|.
gi 1867157819   96 KLYRMGQHY--EEEKRALSHE 114
Cdd:PRK04863  1042 ELQDLGVPAdsGAEERARARR 1062
 
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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