NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462628929|ref|XP_054182776|]
View 

MAP7 domain-containing protein 2 isoform X4 [Homo sapiens]

Protein Classification

MAP7 domain-containing protein( domain architecture ID 12064852)

MAP7 domain-containing protein such as MAP7D1 (microtubule-associated protein 7 domain containing 1) identified as a novel substrate of doublecortin-like kinase 1 (DCLK1)

Gene Ontology:  GO:0005737

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
419-585 7.56e-28

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: 109.75  E-value: 7.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929 419 KPTAGTTDAGEAAKILAEKRRQARLQKEQEEQERLEKEEQDRLEREELKRKAEEERLRLEEEARKQEEERKRqeeekkkq 498
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRR-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929 499 egeekrkagEEAKRKAEEELLLKEKQEQEKQEKAMIEKQKEAAETKAREVAEQMRLEREQIMLQIEQERLERKKRIDEIM 578
Cdd:pfam05672  73 ---------EEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIM 143

                  ....*..
gi 2462628929 579 KRTRKSD 585
Cdd:pfam05672 144 KRTRKSD 150
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
9-102 5.00e-06

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


The actual alignment was detected with superfamily member pfam17380:

Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 50.12  E-value: 5.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929   9 ERQRLAKERREEREKCLAAREQQILEkQKRARLQYEKQMEERWRKL-EEQRQREdqkraAVEEKRKQKLREEEERLEAMM 87
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIyEEERRRE-----AEEERRKQQEMEERRRIQEQM 558
                          90
                  ....*....|....*
gi 2462628929  88 RRSLERTQQLELKKK 102
Cdd:pfam17380 559 RKATEERSRLEAMER 573
 
Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
419-585 7.56e-28

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: 109.75  E-value: 7.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929 419 KPTAGTTDAGEAAKILAEKRRQARLQKEQEEQERLEKEEQDRLEREELKRKAEEERLRLEEEARKQEEERKRqeeekkkq 498
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRR-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929 499 egeekrkagEEAKRKAEEELLLKEKQEQEKQEKAMIEKQKEAAETKAREVAEQMRLEREQIMLQIEQERLERKKRIDEIM 578
Cdd:pfam05672  73 ---------EEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIM 143

                  ....*..
gi 2462628929 579 KRTRKSD 585
Cdd:pfam05672 144 KRTRKSD 150
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
9-102 5.00e-06

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: 50.12  E-value: 5.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929   9 ERQRLAKERREEREKCLAAREQQILEkQKRARLQYEKQMEERWRKL-EEQRQREdqkraAVEEKRKQKLREEEERLEAMM 87
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIyEEERRRE-----AEEERRKQQEMEERRRIQEQM 558
                          90
                  ....*....|....*
gi 2462628929  88 RRSLERTQQLELKKK 102
Cdd:pfam17380 559 RKATEERSRLEAMER 573
PTZ00121 PTZ00121
MAEBL; Provisional
6-102 1.03e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929    6 KSDERQRLAKERREEREKCLAAREQQILEKQKRARL-------QYEKQME-ERWRKLEEQRQREDQKRAAVEEKRKQKLR 77
Cdd:PTZ00121  1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIeevmklyEEEKKMKaEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
                           90       100
                   ....*....|....*....|....*
gi 2462628929   78 EEEERLEAMMRRSLERTQQLELKKK 102
Cdd:PTZ00121  1639 KKKEAEEKKKAEELKKAEEENKIKA 1663
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
9-102 2.81e-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: 40.60  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929   9 ERQRLAKERREEREkclaAREQQILEKQKRARLQYEKQMEERWRKLEEQR-QREDQKRAAVEEKRKQKLREEEERLEAMM 87
Cdd:TIGR02794  66 EQERQKKLEQQAEE----AEKQRAAEQARQKELEQRAAAEKAAKQAEQAAkQAEEKQKQAEEAKAKQAAEAKAKAEAEAE 141
                          90
                  ....*....|....*.
gi 2462628929  88 RRSLERTQ-QLELKKK 102
Cdd:TIGR02794 142 RKAKEEAAkQAEEEAK 157
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
9-75 3.79e-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: 39.87  E-value: 3.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462628929   9 ERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQRE-----DQKRAAVEEKRKQK 75
Cdd:cd16269   197 EKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEErenllKEQERALESKLKEQ 268
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
9-98 9.74e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 9.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929   9 ERQRLAKERREEREKCLAAREQQILEKQKRARLQyekQMEERWRKLEEQRQREDQKRAAVEEKRKQKLREEEERLEAMMR 88
Cdd:COG4717   109 AELEELREELEKLEKLLQLLPLYQELEALEAELA---ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQ 185
                          90
                  ....*....|
gi 2462628929  89 RSLERTQQLE 98
Cdd:COG4717   186 LSLATEEELQ 195
 
Name Accession Description Interval E-value
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
419-585 7.56e-28

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: 109.75  E-value: 7.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929 419 KPTAGTTDAGEAAKILAEKRRQARLQKEQEEQERLEKEEQDRLEREELKRKAEEERLRLEEEARKQEEERKRqeeekkkq 498
Cdd:pfam05672   1 KPSAGTTDAEEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRR-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929 499 egeekrkagEEAKRKAEEELLLKEKQEQEKQEKAMIEKQKEAAETKAREVAEQMRLEREQIMLQIEQERLERKKRIDEIM 578
Cdd:pfam05672  73 ---------EEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKIMQQEEQERLERKKRIEEIM 143

                  ....*..
gi 2462628929 579 KRTRKSD 585
Cdd:pfam05672 144 KRTRKSD 150
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
9-102 5.00e-06

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: 50.12  E-value: 5.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929   9 ERQRLAKERREEREKCLAAREQQILEkQKRARLQYEKQMEERWRKL-EEQRQREdqkraAVEEKRKQKLREEEERLEAMM 87
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIyEEERRRE-----AEEERRKQQEMEERRRIQEQM 558
                          90
                  ....*....|....*
gi 2462628929  88 RRSLERTQQLELKKK 102
Cdd:pfam17380 559 RKATEERSRLEAMER 573
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
9-104 6.57e-04

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: 40.80  E-value: 6.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929   9 ERQRLAKERRE--EREKCLAAREQQILEKQKRA-RLQYEKQMEERWRKLEE-QRQREDQKRAAVEEKRKQKlrEEEERLE 84
Cdd:pfam15346  46 ARKIMEKQVLEelEREREAELEEERRKEEEERKkREELERILEENNRKIEEaQRKEAEERLAMLEEQRRMK--EERQRRE 123
                          90       100
                  ....*....|....*....|
gi 2462628929  85 AMMRRSLERTQQLELKKKYS 104
Cdd:pfam15346 124 KEEEEREKREQQKILNKKNS 143
PTZ00121 PTZ00121
MAEBL; Provisional
6-102 1.03e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929    6 KSDERQRLAKERREEREKCLAAREQQILEKQKRARL-------QYEKQME-ERWRKLEEQRQREDQKRAAVEEKRKQKLR 77
Cdd:PTZ00121  1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIeevmklyEEEKKMKaEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
                           90       100
                   ....*....|....*....|....*
gi 2462628929   78 EEEERLEAMMRRSLERTQQLELKKK 102
Cdd:PTZ00121  1639 KKKEAEEKKKAEELKKAEEENKIKA 1663
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
9-96 2.69e-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: 39.25  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929   9 ERQRLAKER--REEREKclaaREQQILEKQKRARLQyEKQMEERWRKLEEQRQREDQKRAAvEEKRKQKLREEEERLEAM 86
Cdd:pfam05672  18 EKRRQAREQreREEQER----LEKEEEERLRKEELR-RRAEEERARREEEARRLEEERRRE-EEERQRKAEEEAEEREQR 91
                          90
                  ....*....|
gi 2462628929  87 MRRSLERTQQ 96
Cdd:pfam05672  92 EQEEQERLQK 101
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
8-75 2.75e-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: 40.67  E-value: 2.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462628929   8 DERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQK 75
Cdd:pfam13868  58 EEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
9-102 2.81e-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: 40.60  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929   9 ERQRLAKERREEREkclaAREQQILEKQKRARLQYEKQMEERWRKLEEQR-QREDQKRAAVEEKRKQKLREEEERLEAMM 87
Cdd:TIGR02794  66 EQERQKKLEQQAEE----AEKQRAAEQARQKELEQRAAAEKAAKQAEQAAkQAEEKQKQAEEAKAKQAAEAKAKAEAEAE 141
                          90
                  ....*....|....*.
gi 2462628929  88 RRSLERTQ-QLELKKK 102
Cdd:TIGR02794 142 RKAKEEAAkQAEEEAK 157
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
9-102 3.15e-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: 40.88  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929   9 ERQRLAKERREEREkclAAREQQILEKQK------------RARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQKL 76
Cdd:pfam17380 386 ERQQKNERVRQELE---AARKVKILEEERqrkiqqqkvemeQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQV 462
                          90       100
                  ....*....|....*....|....*.
gi 2462628929  77 REEEERLEAMMRRSLERTQQLELKKK 102
Cdd:pfam17380 463 ERLRQQEEERKRKKLELEKEKRDRKR 488
rne PRK10811
ribonuclease E; Reviewed
9-151 3.36e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 41.18  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929    9 ERQRlaKERREEREKCLAAREQQILEKQKRARLQYEKQMEERwrkLEEQRQREDQKRAA--------VEEKRKQKLREEE 80
Cdd:PRK10811   637 EENR--RNRRQAQQQTAETRESQQAEVTEKARTQDEQQQAPR---RERQRRRNDEKRQAqqeakalnVEEQSVQETEQEE 711
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462628929   81 ERLEAMMRRsleRTQQLELKKKY-SWGAPLAIGPGGHDGESENT-----PPPPLGLAASTLPPDAGTTAAAAESTNA 151
Cdd:PRK10811   712 RVQQVQPRR---KQRQLNQKVRIeQSVAEEAVAPVVEETVAAEPvvqevPAPRTELVKVPLPVVAQTAPEQDEENNA 785
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
6-75 3.47e-03

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 39.25  E-value: 3.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929   6 KSDERQRLAKERREEREKclaarEQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQK 75
Cdd:pfam09756   6 KKRAKLELKEAKRQQREA-----EEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQERK 70
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
9-75 3.79e-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: 39.87  E-value: 3.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462628929   9 ERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQRE-----DQKRAAVEEKRKQK 75
Cdd:cd16269   197 EKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEErenllKEQERALESKLKEQ 268
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
10-63 4.06e-03

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 39.25  E-value: 4.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462628929  10 RQRLAKER-REEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQ 63
Cdd:pfam09756  19 QQREAEEEeREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQE 73
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
9-101 4.90e-03

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: 40.02  E-value: 4.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929   9 ERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQM---EERWRKL----EEQRQREDQKRAAVEEKRKQKLREEEE 81
Cdd:pfam15558  51 ERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQViekESRWREQaedqENQRQEKLERARQEAEQRKQCQEQRLK 130
                          90       100
                  ....*....|....*....|
gi 2462628929  82 RLEAMMRRSLERTQQLELKK 101
Cdd:pfam15558 131 EKEEELQALREQNSLQLQER 150
PTZ00121 PTZ00121
MAEBL; Provisional
6-74 4.90e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.90e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929    6 KSDERQRLAKE-RREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQ 74
Cdd:PTZ00121  1669 KAEEDKKKAEEaKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
4-74 5.58e-03

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: 39.63  E-value: 5.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462628929   4 FLKSDER-QRLAKER-REEREKclAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQ 74
Cdd:pfam15558 206 LQRSQENyEQLVEERhRELREK--AQKEEEQFQRAKWRAEEKEEERQEHKEALAELADRKIQQARQVAHKTVQ 276
PTZ00121 PTZ00121
MAEBL; Provisional
6-102 5.75e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 5.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929    6 KSDERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQKLREEEERLEA 85
Cdd:PTZ00121  1451 KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
                           90
                   ....*....|....*..
gi 2462628929   86 MMRRSLERTQQLELKKK 102
Cdd:PTZ00121  1531 EEAKKADEAKKAEEKKK 1547
PTZ00121 PTZ00121
MAEBL; Provisional
6-102 6.21e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 6.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929    6 KSDERQRLAKE-RREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQKLREEEERLE 84
Cdd:PTZ00121  1641 KEAEEKKKAEElKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
                           90
                   ....*....|....*...
gi 2462628929   85 AMMRRSLERTQQLELKKK 102
Cdd:PTZ00121  1721 LKKAEEENKIKAEEAKKE 1738
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
8-74 7.19e-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: 39.52  E-value: 7.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929   8 DERQRLAKERREEREKCLA---AREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQ 74
Cdd:pfam13868  40 EEERRLDEMMEEERERALEeeeEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVER 109
PTZ00121 PTZ00121
MAEBL; Provisional
6-102 8.71e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 8.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929    6 KSDERQRLAKERREEREKCLAAREQQILEKQKRARLQYEKQMEERWRKLEEQRQREDQKRAAVEEKRKQKLREEEERLEA 85
Cdd:PTZ00121  1290 KKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
                           90
                   ....*....|....*..
gi 2462628929   86 MMRRSLERTQQLELKKK 102
Cdd:PTZ00121  1370 EKKKEEAKKKADAAKKK 1386
RIB43A pfam05914
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar ...
19-103 8.74e-03

RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar microtubules contain a specialized set of protofilaments, termed ribbons, that are composed of tubulin and several associated proteins. RIB43A was first characterized in the unicellular biflagellate, Chlamydomonas reinhardtii although highly related sequences are present in several higher eukaryotes including humans. The function of this protein is unknown although the structure of RIB43A and its association with the specialized protofilament ribbons and with basal bodies is relevant to the proposed role of ribbons in forming and stabilising doublet and triplet microtubules and in organizing their three-dimensional structure. Human RIB43A homologs could represent a structural requirement in centriole replication in dividing cells.


Pssm-ID: 461780 [Multi-domain]  Cd Length: 372  Bit Score: 39.11  E-value: 8.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929  19 EEREKCLAAREQQILEKQKRarLQYEKQMEERWrkleeQRQREDQKRAAVEEKRKQKlreeeeRLEAMMRRSLERT---- 94
Cdd:pfam05914 273 EQLKEIRKEQEQQREEKERR--REEEKQRDAEW-----DRQRLELARAALLLEREQQ------RLRRELRRQLDEEnlql 339
                          90
                  ....*....|
gi 2462628929  95 -QQLELKKKY 103
Cdd:pfam05914 340 aQEQKARQEY 349
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
6-75 9.31e-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: 9.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929   6 KSDERQRLAKERREEREKCLAA---REQQIL------EKQKRARLQYEKQMEERWRKLEEQR-----QREDQKRAAVEEK 71
Cdd:pfam17380 433 RQREVRRLEEERAREMERVRLEeqeRQQQVErlrqqeEERKRKKLELEKEKRDRKRAEEQRRkilekELEERKQAMIEEE 512

                  ....
gi 2462628929  72 RKQK 75
Cdd:pfam17380 513 RKRK 516
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
9-98 9.74e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 9.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462628929   9 ERQRLAKERREEREKCLAAREQQILEKQKRARLQyekQMEERWRKLEEQRQREDQKRAAVEEKRKQKLREEEERLEAMMR 88
Cdd:COG4717   109 AELEELREELEKLEKLLQLLPLYQELEALEAELA---ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQ 185
                          90
                  ....*....|
gi 2462628929  89 RSLERTQQLE 98
Cdd:COG4717   186 LSLATEEELQ 195
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH