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Conserved domains on  [gi|578837017|ref|XP_006724233|]
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GRAM domain-containing protein 4 isoform X5 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PH-GRAM_GRAMDC4 cd13221
GRAM domain-containing protein 4 (GRAMDC4) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 460-565 3.56e-55

GRAM domain-containing protein 4 (GRAMDC4) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; GRAMDC4 is a membrane protein. Nothing is known about its function. Paralogs include: GRAMDC1A, GRAMDC1B, GRAMDC1C, GRAMDC2, GRAMDC3, and GRAMDC-like proteins. It contains a single PH-GRAM domain at its N-terminus. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


:

Pssm-ID: 270041  Cd Length: 104  Bit Score: 181.77  E-value: 3.56e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837017 460 LAVCENGWRCCLINRDrKMPTDYIRNGVLYVTENYLCFESSKSgSSKRNKVIKLVDITDIQKYKVLSVLPGSGMGIAVST 539
Cdd:cd13221    1 LPVWENGWRCCLINRD-KMPTDYIRNGRLYLTENYLCFESSSS-SSKKNVVIPLTDITRIEKAKPYSFLPGSGMSIEVSV 78

                         90       100
                 ....*....|....*....|....*.
gi 578837017 540 PSTQKPLVFGAMVHRDEAFETILSQY 565
Cdd:cd13221   79 SSADKPLFFGAMFRRDEFFDIIALGA 104
tolA super family cl35847
cell envelope integrity inner membrane protein TolA; Provisional
 96-151 2.55e-04

cell envelope integrity inner membrane protein TolA; Provisional


The actual alignment was detected with superfamily member PRK09510:

Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 43.64  E-value: 2.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837017  96 EELRKLREETNAEMLRQELDRERQRRMELEQ-KVQEVLKARTEEQMAQQPPKGQAQA 151
Cdd:PRK09510  78 EEQRKKKEQQQAEELQQKQAAEQERLKQLEKeRLAAQEQKKQAEEAAKQAALKQKQA 134
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 95-213 1.15e-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: 41.37  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837017   95 QEELRKLREETNAEMLRQELDRERQRRMELEQKVQEVLKARTEEQMAQQPPKGQAQAsngAERRSQGLSSRLQKWFYERF 174
Cdd:TIGR02794  65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQA---EEAKAKQAAEAKAKAEAEAE 141

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 578837017  175 GEYVEDFRFQPEENTVETEEPLSARRLTENMRRLKRGAK 213
Cdd:TIGR02794 142 RKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAK 180
 
Name Accession Description Interval E-value
PH-GRAM_GRAMDC4 cd13221
GRAM domain-containing protein 4 (GRAMDC4) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 460-565 3.56e-55

GRAM domain-containing protein 4 (GRAMDC4) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; GRAMDC4 is a membrane protein. Nothing is known about its function. Paralogs include: GRAMDC1A, GRAMDC1B, GRAMDC1C, GRAMDC2, GRAMDC3, and GRAMDC-like proteins. It contains a single PH-GRAM domain at its N-terminus. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 270041  Cd Length: 104  Bit Score: 181.77  E-value: 3.56e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837017 460 LAVCENGWRCCLINRDrKMPTDYIRNGVLYVTENYLCFESSKSgSSKRNKVIKLVDITDIQKYKVLSVLPGSGMGIAVST 539
Cdd:cd13221    1 LPVWENGWRCCLINRD-KMPTDYIRNGRLYLTENYLCFESSSS-SSKKNVVIPLTDITRIEKAKPYSFLPGSGMSIEVSV 78

                         90       100
                 ....*....|....*....|....*.
gi 578837017 540 PSTQKPLVFGAMVHRDEAFETILSQY 565
Cdd:cd13221   79 SSADKPLFFGAMFRRDEFFDIIALGA 104
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 446-568 2.92e-21

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 88.96  E-value: 2.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837017  446 NFHEIFNLTENERPLAVCengwrCCLINRDRkmptdYIRNGVLYVTENYLCFESSKSGSSKRnKVIKLVDITDIQKYKVL 525
Cdd:pfam02893   2 LFRKKFKLPPEERLIASY-----SCYLNRDG-----GPVQGRLYLTNYRLCFRSLPKGWSTK-VVIPLVDIEEIEKLKGG 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 578837017  526 SVLPGSGMGIAVSTPStqkPLVFGAMVHRDEAFETILSQYIKI 568
Cdd:pfam02893  71 ANLFPNGIQVETGSND---KFSFAGFVTRDEAIEFILALLKNA 110
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
452-523 1.49e-09

domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 54.14  E-value: 1.49e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578837017   452 NLTENERPLAVcengWRCCLINrdrkmptDYIRNGVLYVTENYLCFESSKSGSSKrNKVIKLVDITDIQKYK 523
Cdd:smart00568   1 KLPEEEKLIAD----YSCYLSR-------TGPVQGRLYISNYRLCFRSNLPGKLT-KVVIPLADITRIEKST 60
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 96-151 2.55e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 43.64  E-value: 2.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837017  96 EELRKLREETNAEMLRQELDRERQRRMELEQ-KVQEVLKARTEEQMAQQPPKGQAQA 151
Cdd:PRK09510  78 EEQRKKKEQQQAEELQQKQAAEQERLKQLEKeRLAAQEQKKQAEEAAKQAALKQKQA 134
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 95-213 1.15e-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: 41.37  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837017   95 QEELRKLREETNAEMLRQELDRERQRRMELEQKVQEVLKARTEEQMAQQPPKGQAQAsngAERRSQGLSSRLQKWFYERF 174
Cdd:TIGR02794  65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQA---EEAKAKQAAEAKAKAEAEAE 141

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 578837017  175 GEYVEDFRFQPEENTVETEEPLSARRLTENMRRLKRGAK 213
Cdd:TIGR02794 142 RKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAK 180
Caldesmon pfam02029
Caldesmon;
96-236 6.22e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 39.47  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837017   96 EELRKLREETNaemlRQELDRERQRRMELEQKVQEVL-------KARTEEQMAQQPPKGQAQASNGAERRsqglssRLQK 168
Cdd:pfam02029 251 EELRRRRQEKE----SEEFEKLRQKQQEAELELEELKkkreerrKLLEEEEQRRKQEEAERKLREEEEKR------RMKE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837017  169 WFYERFGEYVEDFRFQPEENTVETEEPL-------SARRLTENMRRLKRGAKPVTNFVKN-----LSALSDWYSVYTSAI 236
Cdd:pfam02029 321 EIERRRAEAAEKRQKLPEDSSSEGKKPFkcfspkgSSLKITERAEFLNKSLQKSSSVKKThppavVSKIDSRLEQYTSAI 400
 
Name Accession Description Interval E-value
PH-GRAM_GRAMDC4 cd13221
GRAM domain-containing protein 4 (GRAMDC4) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 460-565 3.56e-55

GRAM domain-containing protein 4 (GRAMDC4) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; GRAMDC4 is a membrane protein. Nothing is known about its function. Paralogs include: GRAMDC1A, GRAMDC1B, GRAMDC1C, GRAMDC2, GRAMDC3, and GRAMDC-like proteins. It contains a single PH-GRAM domain at its N-terminus. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 270041  Cd Length: 104  Bit Score: 181.77  E-value: 3.56e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837017 460 LAVCENGWRCCLINRDrKMPTDYIRNGVLYVTENYLCFESSKSgSSKRNKVIKLVDITDIQKYKVLSVLPGSGMGIAVST 539
Cdd:cd13221    1 LPVWENGWRCCLINRD-KMPTDYIRNGRLYLTENYLCFESSSS-SSKKNVVIPLTDITRIEKAKPYSFLPGSGMSIEVSV 78

                         90       100
                 ....*....|....*....|....*.
gi 578837017 540 PSTQKPLVFGAMVHRDEAFETILSQY 565
Cdd:cd13221   79 SSADKPLFFGAMFRRDEFFDIIALGA 104
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 446-568 2.92e-21

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 88.96  E-value: 2.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837017  446 NFHEIFNLTENERPLAVCengwrCCLINRDRkmptdYIRNGVLYVTENYLCFESSKSGSSKRnKVIKLVDITDIQKYKVL 525
Cdd:pfam02893   2 LFRKKFKLPPEERLIASY-----SCYLNRDG-----GPVQGRLYLTNYRLCFRSLPKGWSTK-VVIPLVDIEEIEKLKGG 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 578837017  526 SVLPGSGMGIAVSTPStqkPLVFGAMVHRDEAFETILSQYIKI 568
Cdd:pfam02893  71 ANLFPNGIQVETGSND---KFSFAGFVTRDEAIEFILALLKNA 110
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 463-565 4.00e-13

Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275393  Cd Length: 94  Bit Score: 65.48  E-value: 4.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837017 463 CENGWRCCLINRDRKMPtdyiRNGVLYVTENYLCFESSKSGsSKRNKVIKLVDITDIQKYKVLSVLPgSGMGIAVSTPST 542
Cdd:cd10570    2 EKLGVRFCCALRPRKLP----LEGTLYLSTYRLIFSSKADG-DETKLVIPLVDITDVEKIAGASFLP-SGLIITCKDFRT 75

                         90       100
                 ....*....|....*....|...
gi 578837017 543 QKPLVFGAMvhrdEAFETILSQY 565
Cdd:cd10570   76 IKFSFDSED----EAVKVIARVL 94
PH-GRAM_GRAMDC cd13220
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 486-564 8.30e-11

GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; The GRAMDC proteins are membrane proteins. Nothing is known about its function. Members include: GRAMDC1A, GRAMDC1B, GRAMDC1C, GRAMDC2, GRAMDC3, GRAMDC4, and GRAMDC-like proteins. All of the members, except for GRAMDC4 are included in this hierarchy. Each contains a single PH-GRAM domain at their N-terminus. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275406  Cd Length: 94  Bit Score: 58.67  E-value: 8.30e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578837017 486 GVLYVTENYLCFESSKSGsSKRNKVIKLVDITDIQKYKVLSVLPGSgmgIAVSTPSTQkpLVFGAMVHRDEAFETILSQ 564
Cdd:cd13220   21 GRLYISENHLCFYSNIFG-WETKLVIPFKDITSIEKKKTALIFPNA---IEITTKGEK--YFFTSFLSRDSAYKLLTRV 93
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
452-523 1.49e-09

domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 54.14  E-value: 1.49e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578837017   452 NLTENERPLAVcengWRCCLINrdrkmptDYIRNGVLYVTENYLCFESSKSGSSKrNKVIKLVDITDIQKYK 523
Cdd:smart00568   1 KLPEEEKLIAD----YSCYLSR-------TGPVQGRLYISNYRLCFRSNLPGKLT-KVVIPLADITRIEKST 60
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 96-151 2.55e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 43.64  E-value: 2.55e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578837017  96 EELRKLREETNAEMLRQELDRERQRRMELEQ-KVQEVLKARTEEQMAQQPPKGQAQA 151
Cdd:PRK09510  78 EEQRKKKEQQQAEELQQKQAAEQERLKQLEKeRLAAQEQKKQAEEAAKQAALKQKQA 134
PTZ00121 PTZ00121
MAEBL; Provisional
 96-201 1.06e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837017   96 EELRKLREETNAEMLRQEldrERQRRMELEQKVQEVLKArtEEQMAQQPPKGQAQASNGAERRSQGLSSRLQKWFYERFG 175
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKA---EEKKKADELKKAEELKKA--EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599

                          90       100
                  ....*....|....*....|....*.
gi 578837017  176 EYVEDFRFQPEENTVETEEPLSARRL 201
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEEL 1625
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 95-213 1.15e-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: 41.37  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837017   95 QEELRKLREETNAEMLRQELDRERQRRMELEQKVQEVLKARTEEQMAQQPPKGQAQAsngAERRSQGLSSRLQKWFYERF 174
Cdd:TIGR02794  65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQA---EEAKAKQAAEAKAKAEAEAE 141

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 578837017  175 GEYVEDFRFQPEENTVETEEPLSARRLTENMRRLKRGAK 213
Cdd:TIGR02794 142 RKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAK 180
PH-GRAM1_TCB1D9_TCB1D9B cd13351
TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin ...
 465-559 1.25e-03

TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 1; TBC1D9 and TCB1D9B may act as a GTPase-activating proteins for Rab family protein(s). TBC1D9 and TCB1D9B contain two N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the first repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275420  Cd Length: 99  Bit Score: 38.53  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837017 465 NGWRCCLINRdrKMPtdyiRNGVLYVTENYLCFESSKSGSSKRnKVIKLVDITDIQKYKVLsVLPGSgmgIAVSTPStqK 544
Cdd:cd13351    6 NYYSCSYWKG--RVP----RQGWLYLSVNHLCFYSFLLGKEAK-LVIRWTDVTQLEKNNSL-LLPDS---IKVVTRD--K 72

                         90
                 ....*....|....*
gi 578837017 545 PLVFGAMVHRDEAFE 559
Cdd:cd13351   73 EHYFSMFLNISETFK 87
Caldesmon pfam02029
Caldesmon;
96-236 6.22e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 39.47  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837017   96 EELRKLREETNaemlRQELDRERQRRMELEQKVQEVL-------KARTEEQMAQQPPKGQAQASNGAERRsqglssRLQK 168
Cdd:pfam02029 251 EELRRRRQEKE----SEEFEKLRQKQQEAELELEELKkkreerrKLLEEEEQRRKQEEAERKLREEEEKR------RMKE 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578837017  169 WFYERFGEYVEDFRFQPEENTVETEEPL-------SARRLTENMRRLKRGAKPVTNFVKN-----LSALSDWYSVYTSAI 236
Cdd:pfam02029 321 EIERRRAEAAEKRQKLPEDSSSEGKKPFkcfspkgSSLKITERAEFLNKSLQKSSSVKKThppavVSKIDSRLEQYTSAI 400
 
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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