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Conserved domains on  [gi|154415887|ref|XP_001580967|]
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lung adenoma susceptibility 1-related family [Trichomonas vaginalis G3]

Protein Classification

DUF814 domain-containing protein( domain architecture ID 12175428)

DUF814 domain-containing protein similar to vertebrates coiled-coil domain-containing protein 25, yeast protein JLP2, and bacterial fibronectin/fibrinogen-binding protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
47-246 2.02e-52

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


:

Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 178.32  E-value: 2.02e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887   47 ARLKREkaEQERLEQEKlEAAKKAQQEKEEESRKR--AEQQQRLEEEKEYIKNFRLQKEEKIQKIVANFEKTEDWELFSQ 124
Cdd:pfam15927   1 ARLREE--EEERLRAEE-EEAERLEEERREEEEEErlAAEQDRRAEELEELKHLLEERKEALEKLRAEAREEAEWERYMR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887  125 CSHAIDVRSEADVNTFISQLSEVNETDINQLFEHIHLAKVIENQLRER-SEKAQLANRVPLYTRCNRQIDTLQQLINQKI 203
Cdd:pfam15927  78 CDGLPDPRDEQEINTFISLWREEEEEDIDEVMETCTLVLELIEELEELlLDTPPEELAEKYVEQYKEVILVLRELINKKI 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 154415887  204 ENITVNHLAFSDKFSGAKGDVQINGGSDD-ITYGMWVNLSKNPR 246
Cdd:pfam15927 158 DEATAHLLRQADEYADRETGNMQKVVKDGnITLCLWANLKKNPR 201
Casc1_C super family cl13761
Cancer susceptibility candidate 1 C-terminal; This is the C-terminal domain of Cancer ...
376-417 8.83e-03

Cancer susceptibility candidate 1 C-terminal; This is the C-terminal domain of Cancer susceptibility candidate 1 (Casc1) which has many SNPs associated with cancer susceptibility.


The actual alignment was detected with superfamily member pfam12366:

Pssm-ID: 432508  Cd Length: 222  Bit Score: 38.20  E-value: 8.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 154415887  376 EDNDVLFSSNLIGTFGLAVPRYRHFPFQFWEISSQSPTSVEI 417
Cdd:pfam12366  18 ETLTLTIKTDRLGIFGFAFKRYEHFPFRDWSLQPNEENPEEI 59
 
Name Accession Description Interval E-value
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
47-246 2.02e-52

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 178.32  E-value: 2.02e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887   47 ARLKREkaEQERLEQEKlEAAKKAQQEKEEESRKR--AEQQQRLEEEKEYIKNFRLQKEEKIQKIVANFEKTEDWELFSQ 124
Cdd:pfam15927   1 ARLREE--EEERLRAEE-EEAERLEEERREEEEEErlAAEQDRRAEELEELKHLLEERKEALEKLRAEAREEAEWERYMR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887  125 CSHAIDVRSEADVNTFISQLSEVNETDINQLFEHIHLAKVIENQLRER-SEKAQLANRVPLYTRCNRQIDTLQQLINQKI 203
Cdd:pfam15927  78 CDGLPDPRDEQEINTFISLWREEEEEDIDEVMETCTLVLELIEELEELlLDTPPEELAEKYVEQYKEVILVLRELINKKI 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 154415887  204 ENITVNHLAFSDKFSGAKGDVQINGGSDD-ITYGMWVNLSKNPR 246
Cdd:pfam15927 158 DEATAHLLRQADEYADRETGNMQKVVKDGnITLCLWANLKKNPR 201
PTZ00121 PTZ00121
MAEBL; Provisional
50-178 3.47e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 3.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887   50 KREKAEQERLEQEKLEAAKKAQQEKEEESRKRAEQQQRLEEEKEyiKNFRLQKEEKIQKIVANFEKTEDWElfsQCSHAI 129
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK--KAEELKKAEEENKIKAEEAKKEAEE---DKKKAE 1747
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 154415887  130 DVRSEADVNTFISQLSEVNETDINQLFEHIHlaKVIENQLRERSEKAQL 178
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE--AVIEEELDEEDEKRRM 1794
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
50-179 4.05e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.42  E-value: 4.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887    50 KREKAEQERLEQEKLEAAKKAQQEKEEESRKRaEQQQRLEEEKEYIKNFR--LQKEEKIQKIVANF---EKTEDWELFSQ 124
Cdd:TIGR00618  431 KQQELQQRYAELCAAAITCTAQCEKLEKIHLQ-ESAQSLKEREQQLQTKEqiHLQETRKKAVVLARlleLQEEPCPLCGS 509
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 154415887   125 CSHAIDVRSEADVNTFISQLSEVNETDINQLFEHI----HLAKVIENQLRERSEKAQLA 179
Cdd:TIGR00618  510 CIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEedvyHQLTSERKQRASLKEQMQEI 568
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
47-179 1.31e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887  47 ARLKREKAEQERLEQEKLEAAKKAQQEKEEESRKRAEQQQRLEEEKEYIKNFRLQKEEKIQKIVANFEKTEDWELFSQcs 126
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE-- 386
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 154415887 127 haIDVRSEADVNTFISQLSEVNETDINQLFEHIHLAKVIENQLRERSEKAQLA 179
Cdd:COG1196  387 --ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
53-115 1.57e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.02  E-value: 1.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154415887  53 KAEQERLEQEKLEAAKKAQQEKEEESRKRAEQQQRLEEEKeyIKNFRLQKEEKIQKIVANFEK 115
Cdd:cd16269  188 QADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQK--LEDQERSYEEHLRQLKEKMEE 248
Casc1_C pfam12366
Cancer susceptibility candidate 1 C-terminal; This is the C-terminal domain of Cancer ...
376-417 8.83e-03

Cancer susceptibility candidate 1 C-terminal; This is the C-terminal domain of Cancer susceptibility candidate 1 (Casc1) which has many SNPs associated with cancer susceptibility.


Pssm-ID: 432508  Cd Length: 222  Bit Score: 38.20  E-value: 8.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 154415887  376 EDNDVLFSSNLIGTFGLAVPRYRHFPFQFWEISSQSPTSVEI 417
Cdd:pfam12366  18 ETLTLTIKTDRLGIFGFAFKRYEHFPFRDWSLQPNEENPEEI 59
 
Name Accession Description Interval E-value
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
47-246 2.02e-52

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 178.32  E-value: 2.02e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887   47 ARLKREkaEQERLEQEKlEAAKKAQQEKEEESRKR--AEQQQRLEEEKEYIKNFRLQKEEKIQKIVANFEKTEDWELFSQ 124
Cdd:pfam15927   1 ARLREE--EEERLRAEE-EEAERLEEERREEEEEErlAAEQDRRAEELEELKHLLEERKEALEKLRAEAREEAEWERYMR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887  125 CSHAIDVRSEADVNTFISQLSEVNETDINQLFEHIHLAKVIENQLRER-SEKAQLANRVPLYTRCNRQIDTLQQLINQKI 203
Cdd:pfam15927  78 CDGLPDPRDEQEINTFISLWREEEEEDIDEVMETCTLVLELIEELEELlLDTPPEELAEKYVEQYKEVILVLRELINKKI 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 154415887  204 ENITVNHLAFSDKFSGAKGDVQINGGSDD-ITYGMWVNLSKNPR 246
Cdd:pfam15927 158 DEATAHLLRQADEYADRETGNMQKVVKDGnITLCLWANLKKNPR 201
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
47-108 3.06e-08

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 53.12  E-value: 3.06e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 154415887   47 ARLKREKAEQERLEQEKLEaakkaQQEKEEESRKRAEQQQRLEEEKEYIKNFRLQKEEKIQK 108
Cdd:pfam05672  23 AREQREREEQERLEKEEEE-----RLRKEELRRRAEEERARREEEARRLEEERRREEEERQR 79
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
48-107 7.43e-08

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 55.34  E-value: 7.43e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154415887   48 RLKREKAEQERLEQEKLEAAKKAQQEKEEESRKRAEQ----QQRLEEEKEyiknfRLQKEEKIQ 107
Cdd:pfam15709 352 RKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEirlrKQRLEEERQ-----RQEEEERKQ 410
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
54-124 2.80e-05

G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.


Pssm-ID: 464961 [Multi-domain]  Cd Length: 272  Bit Score: 46.07  E-value: 2.80e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154415887   54 AEQERLEQEkLEAAKKAQQEKEEESRKRAEQQQRLEEEKEYIknfrLQKEEKIQKIvanfeKTEDWELFSQ 124
Cdd:pfam15991  20 RERERKKQE-QEAKMEEERLRREREEREKEDRMTLEETKEQI----LKLEKKLADL-----KEEKHQLFLQ 80
PTZ00121 PTZ00121
MAEBL; Provisional
50-178 3.47e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 3.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887   50 KREKAEQERLEQEKLEAAKKAQQEKEEESRKRAEQQQRLEEEKEyiKNFRLQKEEKIQKIVANFEKTEDWElfsQCSHAI 129
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK--KAEELKKAEEENKIKAEEAKKEAEE---DKKKAE 1747
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 154415887  130 DVRSEADVNTFISQLSEVNETDINQLFEHIHlaKVIENQLRERSEKAQL 178
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE--AVIEEELDEEDEKRRM 1794
MRP-S26 pfam14943
Mitochondrial ribosome subunit S26; This family of proteins corresponds to mitochondrial ...
47-112 6.52e-05

Mitochondrial ribosome subunit S26; This family of proteins corresponds to mitochondrial ribosomal subunit S26 in eukaryotes


Pssm-ID: 464391 [Multi-domain]  Cd Length: 168  Bit Score: 43.77  E-value: 6.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154415887   47 ARLKREKAEQERLEQEKLEAAKkAQQEKEEESRKRAEQqqRLEEEKEYIKNF--RLQKEEKIQKIVAN 112
Cdd:pfam14943  90 LREERLAKEAEEREEEILERIE-EKEEKEEEKKERAEE--EVRQEKEESKTFitRENLDAAIEEALDN 154
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
50-112 7.51e-05

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 43.12  E-value: 7.51e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154415887   50 KREKAEQERLEQEKLEAAKKAQQEKEEESRKRAEQQQRLEEEKEYIKNFRLQKEEKIQKIVAN 112
Cdd:pfam15346  77 RKKREELERILEENNRKIEEAQRKEAEERLAMLEEQRRMKEERQRREKEEEEREKREQQKILN 139
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
47-93 1.13e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.53  E-value: 1.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 154415887   47 ARLKREKAEQERLEQEKLEAAKKAQQEKEEESRKRAEQQQRLEEEKE 93
Cdd:pfam03154 581 AGSKLAKKREEALEKAKREAEQKAREEKEREKEKEKERERERERERE 627
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
47-112 1.40e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 44.64  E-value: 1.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 154415887   47 ARLKREKAEQERLEQEKLEAAKkaqqeKEEESRKRaEQQQRLEEEKEYIKNFRLQKEEKIQKIVAN 112
Cdd:pfam15558  94 SRWREQAEDQENQRQEKLERAR-----QEAEQRKQ-CQEQRLKEKEEELQALREQNSLQLQERLEE 153
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
51-117 1.73e-04

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 41.44  E-value: 1.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 154415887   51 REKAEQERLE--------QEKLEAAKKAQQEKEEESRKRAEQQQRLEEEKEYIKNFRLQKEEKIQKIVANFEKTE 117
Cdd:pfam20492   1 REEAEREKQEleerlkqyEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEA 75
PTZ00121 PTZ00121
MAEBL; Provisional
50-151 3.28e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887   50 KREKAEQERLEQEKLEAAKKAQQEKEEESRKRAEQQQRLEEEKEYiKNFRLQKEEKIQKIVANFEKTEDWELfsqcSHAI 129
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK-AAEALKKEAEEAKKAEELKKKEAEEK----KKAE 1719
                          90       100
                  ....*....|....*....|...
gi 154415887  130 DVRSEADVNTF-ISQLSEVNETD 151
Cdd:PTZ00121 1720 ELKKAEEENKIkAEEAKKEAEED 1742
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
52-118 3.90e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 3.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154415887  52 EKAEQERLEQEklEAAKKAQQEKEEESRKRAEQQQRLEEEKEYIKNFRLQKEEKIQKIVANFEKTED 118
Cdd:PRK00409 523 ASLEELERELE--QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEAD 587
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
50-179 4.05e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.42  E-value: 4.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887    50 KREKAEQERLEQEKLEAAKKAQQEKEEESRKRaEQQQRLEEEKEYIKNFR--LQKEEKIQKIVANF---EKTEDWELFSQ 124
Cdd:TIGR00618  431 KQQELQQRYAELCAAAITCTAQCEKLEKIHLQ-ESAQSLKEREQQLQTKEqiHLQETRKKAVVLARlleLQEEPCPLCGS 509
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 154415887   125 CSHAIDVRSEADVNTFISQLSEVNETDINQLFEHI----HLAKVIENQLRERSEKAQLA 179
Cdd:TIGR00618  510 CIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEedvyHQLTSERKQRASLKEQMQEI 568
Pinin_SDK_memA pfam04696
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ...
52-116 5.09e-04

pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.


Pssm-ID: 461396 [Multi-domain]  Cd Length: 130  Bit Score: 40.35  E-value: 5.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154415887   52 EKAEQERLEQEKLEAAKKAQQEKEEESRKRAEQQQRLE--EEKEYIKNFRLQKEEKiQKIVANFEKT 116
Cdd:pfam04696  39 EKRLEEKAKQEKEELEERKREEREELFEERRAEQIELRalEEKLELKELMETWHEN-LKALANFLKT 104
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
48-117 7.43e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 40.41  E-value: 7.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887   48 RLKREKAEQERLEQEKLEAAKKAQQEKEEESRKRAEQQQRLEEEkeyiknfRLQKEEKIQKIVANFEKTE 117
Cdd:pfam05672  88 REQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQE-------RLERKKRIEEIMKRTRKSD 150
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
47-179 1.31e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887  47 ARLKREKAEQERLEQEKLEAAKKAQQEKEEESRKRAEQQQRLEEEKEYIKNFRLQKEEKIQKIVANFEKTEDWELFSQcs 126
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE-- 386
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 154415887 127 haIDVRSEADVNTFISQLSEVNETDINQLFEHIHLAKVIENQLRERSEKAQLA 179
Cdd:COG1196  387 --ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
53-115 1.57e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.02  E-value: 1.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154415887  53 KAEQERLEQEKLEAAKKAQQEKEEESRKRAEQQQRLEEEKeyIKNFRLQKEEKIQKIVANFEK 115
Cdd:cd16269  188 QADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQK--LEDQERSYEEHLRQLKEKMEE 248
PTZ00121 PTZ00121
MAEBL; Provisional
50-120 2.01e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887   50 KREKAEQERLEQE-------KLEAAKKAQQEK--------EEESRKRAEQQQRLEEEKeyIKNFRLQKEEKIQKIVANFE 114
Cdd:PTZ00121 1562 EKKKAEEAKKAEEdknmalrKAEEAKKAEEARieevmklyEEEKKMKAEEAKKAEEAK--IKAEELKKAEEEKKKVEQLK 1639

                  ....*.
gi 154415887  115 KTEDWE 120
Cdd:PTZ00121 1640 KKEAEE 1645
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
48-108 2.12e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 2.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154415887  48 RLKREKAEQERLEQEKleaAKKAQQEKEEESRKRAEQQQRL---EEEKEYIKNFRLQKEEKIQK 108
Cdd:PRK09510  66 RQQQQQKSAKRAEEQR---KKKEQQQAEELQQKQAAEQERLkqlEKERLAAQEQKKQAEEAAKQ 126
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
47-177 2.22e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887  47 ARLKREKAEQERLEQEKLEAAKKAQQEKEEESRKRAEQQQRLEEEKEYIKNFRlQKEEKIQKIVANFEKTEDwELFSQCS 126
Cdd:COG4717  107 LEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQE-ELEELLE 184
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 154415887 127 HaIDVRSEADVNTFISQLSEVNEtDINQLFEHIHLAKVIENQLRERSEKAQ 177
Cdd:COG4717  185 Q-LSLATEEELQDLAEELEELQQ-RLAELEEELEEAQEELEELEEELEQLE 233
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
47-105 2.57e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 40.24  E-value: 2.57e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 154415887   47 ARLKREKAEQERLEQEKLEAAKKAQQEKEEESRKR------AEQQQRLeEEKEYiknfrlQKEEK 105
Cdd:pfam07946 265 TREEEIEKIKKAAEEERAEEAQEKKEEAKKKEREEklaklsPEEQRKY-EEKER------KKEQR 322
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
52-91 2.95e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.71  E-value: 2.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 154415887   52 EKAEQERLE--QEKLEAAKKAQQEKEEEsRKRAEQQQRLEEE 91
Cdd:pfam15709 470 EMAEEERLEyqRQKQEAEEKARLEAEER-RQKEEEAARLALE 510
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
50-115 3.15e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.21  E-value: 3.15e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 154415887   50 KREKAEQERLEQEKLEAAKKAQQEKEEESRKRAEQQQRLEEEKEYIknfrlQKEEKIQKIVANFEK 115
Cdd:TIGR02794  82 KQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK-----QAAEAKAKAEAEAER 142
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
48-105 3.54e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.49  E-value: 3.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154415887   48 RLKREKAEQ----ERLEQEKLE-AAKKAQQEKEEESRKRAEQQQRLEEEKEYIKNFRLQKEEK 105
Cdd:pfam17380 450 RVRLEEQERqqqvERLRQQEEErKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEE 512
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
51-91 3.70e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.17  E-value: 3.70e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 154415887  51 REKAEQERL---EQEKLEAAKkaQQEKEEESRKRAEQQQRLEEE 91
Cdd:PRK09510  95 KQAAEQERLkqlEKERLAAQE--QKKQAEEAAKQAALKQKQAEE 136
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
47-108 3.70e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 3.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 154415887   47 ARLKREKAEQERLEQEKLEAAKKAQQEKEEEsrkRAEQQQRLEEEKEYIKNFRLQKEEKIQK 108
Cdd:pfam13868 140 AEWKELEKEEEREEDERILEYLKEKAEREEE---REAEREEIEEEKEREIARLRAQQEKAQD 198
PTZ00121 PTZ00121
MAEBL; Provisional
47-108 3.73e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 3.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154415887   47 ARLKREKAEQERLEQEKLEAAKKAQQ-EKEEESRKRAEQQQRLEEEKEYIKNFRLQKEEKIQK 108
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
47-105 4.24e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.10  E-value: 4.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887   47 ARLKREKAEQERlEQEKLEAAKKAQQEKEEESRKRAE-QQQRLEEEKeyiknfRLQKEEK 105
Cdd:pfam05672  78 QRKAEEEAEERE-QREQEEQERLQKQKEEAEAKAREEaERQRQEREK------IMQQEEQ 130
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
47-159 5.50e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 5.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887   47 ARLKREKAEQERLEQEkLEAAKKAQQEKEEESRKRAEQQQRLEEEKEYIKNFRLQKEEKIQKIVANFEKTEDWELFSQCS 126
Cdd:COG4913   678 ERLDASSDDLAALEEQ-LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA 756
                          90       100       110
                  ....*....|....*....|....*....|...
gi 154415887  127 HAIDVRSEADVNTFISQLSEVNETDINQLFEHI 159
Cdd:COG4913   757 AALGDAVERELRENLEERIDALRARLNRAEEEL 789
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
51-93 7.82e-03

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 36.82  E-value: 7.82e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 154415887   51 REKAEQERLEQEKLEAAKKAQQeKEEESRKRAEQQQRLEEEKE 93
Cdd:pfam20492  73 MEAEEKEQLEAELAEAQEEIAR-LEEEVERKEEEARRLQEELE 114
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
50-178 8.40e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.34  E-value: 8.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887   50 KREKAEQERLEQEKLEAAKKAQQEKEEESRKRAEQQQRLEEEKEYIKNFRL--QKEEKIQKIVANfEKTEDWELFSQCSH 127
Cdd:pfam17380 292 KFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMamERERELERIRQE-ERKRELERIRQEEI 370
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 154415887  128 AIDVRSEADVNTFISQLSEVNETdINQLFEHIHLAKVIENQlRERSEKAQL 178
Cdd:pfam17380 371 AMEISRMRELERLQMERQQKNER-VRQELEAARKVKILEEE-RQRKIQQQK 419
Casc1_C pfam12366
Cancer susceptibility candidate 1 C-terminal; This is the C-terminal domain of Cancer ...
376-417 8.83e-03

Cancer susceptibility candidate 1 C-terminal; This is the C-terminal domain of Cancer susceptibility candidate 1 (Casc1) which has many SNPs associated with cancer susceptibility.


Pssm-ID: 432508  Cd Length: 222  Bit Score: 38.20  E-value: 8.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 154415887  376 EDNDVLFSSNLIGTFGLAVPRYRHFPFQFWEISSQSPTSVEI 417
Cdd:pfam12366  18 ETLTLTIKTDRLGIFGFAFKRYEHFPFRDWSLQPNEENPEEI 59
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
50-96 9.89e-03

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 37.36  E-value: 9.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 154415887   50 KREKAEQERLEQEKLEAAKKAQQEKEEESRKRaEQQQRLEEEKEYIK 96
Cdd:pfam11600  79 EKEKAEKLRLKEEKRKEKQEALEAKLEEKRKK-EEEKRLKEEEKRIK 124
Cgr1 pfam03879
Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA ...
47-110 9.93e-03

Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA processing.


Pssm-ID: 427562 [Multi-domain]  Cd Length: 107  Bit Score: 36.06  E-value: 9.93e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154415887   47 ARLKREKAEQERLEQEKlEAAKKAQQEKEEESRKRAEQQQRLEEEKEYI---KNFRLQKEEKIQKIV 110
Cdd:pfam03879  40 LELKAIKAKEKELKDEK-EAERQRRIQAIKERREAKEEKERYEELAAKMhakKVERLKRKEKRNKLL 105
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
47-206 9.93e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 9.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887  47 ARLKREKAEQERLE-QEKLEAAKKAQQEKEEESRKRAEQQQRLEEEKEYIKNFRLQKEEKIQKIVanfEKTEDWELFSQC 125
Cdd:COG1196  272 LRLELEELELELEEaQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE---EELEELEEELEE 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154415887 126 SHAIDVRSEADVNTFISQLSEVNETDINQLFEHIHLAKVIENQLRERSEKAQLANRVplytrcNRQIDTLQQLINQKIEN 205
Cdd:COG1196  349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL------EEAEEALLERLERLEEE 422

                 .
gi 154415887 206 I 206
Cdd:COG1196  423 L 423
 
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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