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Conserved domains on  [gi|729728614|ref|XP_010560073|]
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PREDICTED: rab-3A-interacting protein isoform X2 [Haliaeetus leucocephalus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rab11BD_RAB3IP cd21068
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or ...
 235-427 2.08e-150

Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or SSX2-interacting protein, or Rabin8, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. It mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. It modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. The model corresponds to the Rab11a/Rab11b-binding region of RAB3IP lies within its carboxy-terminus, a region distinct from its GEF domain and Rab3a-binding region.


:

Pssm-ID: 411032  Cd Length: 193  Bit Score: 424.33  E-value: 2.08e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729728614 235 GHARNKSTSSAMGGSHQDLTMMQPIVKDCKEADLSLYNEFRSWKDEPTMDRTCPFLDKIYREDIFPCLTFSKSELASAVL 314
Cdd:cd21068    1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKEEPTMDRTCPFLDRIYQEDIFPCLTFSKSELASAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729728614 315 EAVENNTLSIEPVGLQPVRFVKASAVECGGPKKCALSGQSKSCKHRIKLGDSSSYYYISPFCRYRITSVCNFFTYIRYIQ 394
Cdd:cd21068   81 EAVENNTLSIEPVGLQPLRFVKASAVECGGPKKCALSGQTKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 729728614 395 QGLLKQQDVDQMFWEVMQLRREMSLAKLGYYKE 427
Cdd:cd21068  161 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYYKE 193
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 159-209 9.44e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


:

Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 9.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 729728614 159 YERLKEELAKAQREAHKMVKEANVKQAAAEKQLKEAQGKIDVLQAEVAALK 209
Cdd:COG3883  145 LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195
 
Name Accession Description Interval E-value
Rab11BD_RAB3IP cd21068
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or ...
 235-427 2.08e-150

Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or SSX2-interacting protein, or Rabin8, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. It mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. It modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. The model corresponds to the Rab11a/Rab11b-binding region of RAB3IP lies within its carboxy-terminus, a region distinct from its GEF domain and Rab3a-binding region.


Pssm-ID: 411032  Cd Length: 193  Bit Score: 424.33  E-value: 2.08e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729728614 235 GHARNKSTSSAMGGSHQDLTMMQPIVKDCKEADLSLYNEFRSWKDEPTMDRTCPFLDKIYREDIFPCLTFSKSELASAVL 314
Cdd:cd21068    1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKEEPTMDRTCPFLDRIYQEDIFPCLTFSKSELASAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729728614 315 EAVENNTLSIEPVGLQPVRFVKASAVECGGPKKCALSGQSKSCKHRIKLGDSSSYYYISPFCRYRITSVCNFFTYIRYIQ 394
Cdd:cd21068   81 EAVENNTLSIEPVGLQPLRFVKASAVECGGPKKCALSGQTKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 729728614 395 QGLLKQQDVDQMFWEVMQLRREMSLAKLGYYKE 427
Cdd:cd21068  161 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYYKE 193
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 159-209 9.44e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 9.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 729728614 159 YERLKEELAKAQREAHKMVKEANVKQAAAEKQLKEAQGKIDVLQAEVAALK 209
Cdd:COG3883  145 LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 161-210 1.93e-04

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 41.84  E-value: 1.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 729728614  161 RLKEELAKAQR---EAHKMVKEANVKQAAAEKQLKEAQGKIDVLQAEVAALKT 210
Cdd:pfam08614  61 QLREELAELYRsrgELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEE 113
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 160-204 4.89e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.03  E-value: 4.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 729728614 160 ERLKEE----LAKAQREAHKMVKEANvKQAAAEKQ--LKEAQGKIDVLQAE 204
Cdd:cd06503   50 EELLAEyeekLAEARAEAQEIIEEAR-KEAEKIKEeiLAEAKEEAERILEQ 99
 
Name Accession Description Interval E-value
Rab11BD_RAB3IP cd21068
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or ...
 235-427 2.08e-150

Rab11 binding domain of Rab-3A-interacting protein (RAB3IP); RAB3IP, also called Rabin-3, or SSX2-interacting protein, or Rabin8, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. It mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. It modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. The model corresponds to the Rab11a/Rab11b-binding region of RAB3IP lies within its carboxy-terminus, a region distinct from its GEF domain and Rab3a-binding region.


Pssm-ID: 411032  Cd Length: 193  Bit Score: 424.33  E-value: 2.08e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729728614 235 GHARNKSTSSAMGGSHQDLTMMQPIVKDCKEADLSLYNEFRSWKDEPTMDRTCPFLDKIYREDIFPCLTFSKSELASAVL 314
Cdd:cd21068    1 GHARNKSTSSAMSGSHQDLSVIQPIVKDCKEADLSLYNEFRLWKEEPTMDRTCPFLDRIYQEDIFPCLTFSKSELASAVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729728614 315 EAVENNTLSIEPVGLQPVRFVKASAVECGGPKKCALSGQSKSCKHRIKLGDSSSYYYISPFCRYRITSVCNFFTYIRYIQ 394
Cdd:cd21068   81 EAVENNTLSIEPVGLQPLRFVKASAVECGGPKKCALSGQTKSCKHRIKLGDSSNYYYISPFCRYRITSVCNFFTYIRYIQ 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 729728614 395 QGLLKQQDVDQMFWEVMQLRREMSLAKLGYYKE 427
Cdd:cd21068  161 QGLVKQQDVDQMFWEVMQLRKEMSLAKLGYYKE 193
Rab11BD_RAB3IL1 cd21069
Rab11 binding domain of Rab-3A-interacting-like protein 1 (RAB3IL1); RAB3IL1, also called ...
 262-425 6.61e-97

Rab11 binding domain of Rab-3A-interacting-like protein 1 (RAB3IL1); RAB3IL1, also called guanine nucleotide exchange factor for Rab-3A (GRAB), or Rab3A-interacting-like protein 1, or Rabin3-like 1, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. As a dual Rab-binding protein, RAB3IL1 could potentially link Rab3 and Rab11 and/or Rab8 and Rab11-mediated intracellular trafficking processes. It may activate RAB3A, a GTPase that regulates synaptic vesicle exocytosis. It may also activate RAB8A and RAB8B. In addition, RAB3IL1 interacts with InsP6K1 and plays a role for InsP7 in vesicle exocytosis. The model corresponds to the Rab11a/Rab11b-binding region of RAB3IL1 lies within its carboxy-terminus, a region distinct from its GEF domain and Rab3a-binding region.


Pssm-ID: 411033  Cd Length: 163  Bit Score: 287.14  E-value: 6.61e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729728614 262 DCKEADLSLYNEFRSWKDEPTMDRTCPFLDKIYREDIFPCLTFSKSELASAVLEAVENNTLSIEPVGLQPVRFVKASAVE 341
Cdd:cd21069    1 EGKEVDTVLFAEFQAWKESPTLDRSCPFLSRIYREDIGPCLDFTKRELSDLVQSAVENNTLTIEPVASQALPVVKASAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729728614 342 CGGPKKCALSGQSKSCKHRIKLGDSSSYYYISPFCRYRITSVCNFFTYIRYIQQGLLKqQDVDQMFWEVMQLRREMSLAK 421
Cdd:cd21069   81 CGGPKKCALSGLSRTCRHRIKLGDSGNYYYISPSCRARITAVCNFFTYIRYIQQGLVR-QDAEQMFWEVMRLRREMSLAK 159


                 ....
gi 729728614 422 LGYY 425
Cdd:cd21069  160 LGFY 163
Rab11BD_RAB3IP_like cd21044
Rab11 binding domain of Rab-3A-interacting protein (RAB3IP), Rab-3A-interacting-like protein 1 ...
 264-423 2.70e-59

Rab11 binding domain of Rab-3A-interacting protein (RAB3IP), Rab-3A-interacting-like protein 1 (RAB3IL1) and similar proteins; The family includes RAB3IP and RAB3IL1, as well as Rab guanine nucleotide exchange factor SEC2 from yeast. RAB3IP, also called Rabin-3, or SSX2-interacting protein, or Rabin8, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. It mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. It modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. RAB3IL1, also called guanine nucleotide exchange factor for Rab-3A (GRAB), or Rab3A-interacting-like protein 1, or Rabin3-like 1, acts as a guanine nucleotide exchange factor (GEF) which promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. As a dual Rab-binding protein, RAB3IL1 could potentially link Rab3 and Rab11 and/or Rab8 and Rab11-mediated intracellular trafficking processes. It may activate RAB3A, a GTPase that regulates synaptic vesicle exocytosis. It may also activate RAB8A and RAB8B. In addition, RAB3IL1 interacts with InsP6K1 and plays a role for InsP7 in vesicle exocytosis. SEC2 is a guanine nucleotide exchange factor for SEC4, catalyzing the dissociation of GDP from SEC4 and also potently promoting binding of GTP. Activation of SEC4 by SEC2 is needed for the directed transport of vesicles to sites of exocytosis. SEC2 binds the Rab GTPase YPT32 but does not have exchange activity on YPT32. The model corresponds to the Rab11a/Rab11b-binding region of family members which lies within the carboxy-terminus, a region distinct from their GEF domain and Rab3a-binding region.


Pssm-ID: 411031  Cd Length: 178  Bit Score: 191.42  E-value: 2.70e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729728614 264 KEADLSLYNEFRSWKDEP-----TMDRTCPFLDKIYREDIFPCLTFSKS----ELASAVLEAVENNTLSIEPV------G 328
Cdd:cd21044    1 FEVDLVLFEEFQEFLKAPsslslSLLKSSPFLKRILAEDIEPCLRFDPAllnwLLKKRLLAAILENTLEIEPIsgstetS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729728614 329 LQPVRFVKASAVECGGPKKCALSGQSK--SCKHRIKLGDSSS-YYYISPFCRYRITSVCNFFTYIRYIQQGLLKQQDVDQ 405
Cdd:cd21044   81 SSSNNTAPVSSPPPASPKKCALCGESRldACLYRLRLSDSDSeWYPICSYCRNRLRAVCDFFAYLRYIRQGLVKSRSIEK 160

                        170
                 ....*....|....*...
gi 729728614 406 MFWEVMQLRREMSLAKLG 423
Cdd:cd21044  161 LYLEILRLRLRMFLARLG 178
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 159-209 9.44e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 9.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 729728614 159 YERLKEELAKAQREAHKMVKEANVKQAAAEKQLKEAQGKIDVLQAEVAALK 209
Cdd:COG3883  145 LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 161-210 1.93e-04

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 41.84  E-value: 1.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 729728614  161 RLKEELAKAQR---EAHKMVKEANVKQAAAEKQLKEAQGKIDVLQAEVAALKT 210
Cdd:pfam08614  61 QLREELAELYRsrgELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEE 113
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
152-210 3.52e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 3.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 729728614 152 LEVREKGYERLKEELAKAQRE----------AHKMVKEANVKQAAAEKQLKEAQGKIDVLQAEVAALKT 210
Cdd:COG4372   54 LEQAREELEQLEEELEQARSEleqleeeleeLNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 152-209 7.59e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 7.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 729728614 152 LEVREKGYERLKEELAKAQREAHKM---VKEANVKQAAAEKQLKEAQGKIDVLQAEVAALK 209
Cdd:COG3883   18 IQAKQKELSELQAELEAAQAELDALqaeLEELNEEYNELQAELEALQAEIDKLQAEIAEAE 78
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 159-210 9.12e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 9.12e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 729728614 159 YERLKEELAKAQREAHKMVKEANVKQAAAEKQLKEAQGKIDVLQAEVAALKT 210
Cdd:COG3883  138 LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 153-197 1.01e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 41.14  E-value: 1.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 729728614  153 EVREKGYERLKEELAKAQREAHKMVKEANVKQAAAEKQLKEAQGK 197
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQK 253
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 151-209 1.34e-03

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 38.68  E-value: 1.34e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 729728614 151 VLEVREKGYERLKEElakAQREAHKMVKEANVKqaaAEKQLKEAQGKIDVLQAEVAALK 209
Cdd:COG3599   70 TLVVAQETAEEVKEN---AEKEAELIIKEAELE---AEKIIEEAQEKARKIVREIEELK 122
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
152-226 1.70e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729728614 152 LEVREKGYERLKEELAKAQREAHKMVKEANVKQA----------AAEKQLKEAQGKIDVLQAEVAALKTLVLSTSPTSPT 221
Cdd:COG4372  103 LESLQEEAEELQEELEELQKERQDLEQQRKQLEAqiaelqseiaEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182


                 ....*
gi 729728614 222 KEFQS 226
Cdd:COG4372  183 QALDE 187
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 156-209 2.00e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 38.62  E-value: 2.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 729728614 156 EKGYERLKEELAKAQREAHKMVKEAnvkQAAAEKQLKEAQGKidvLQAEVAALK 209
Cdd:COG0711   51 EAALAEYEEKLAEARAEAAEIIAEA---RKEAEAIAEEAKAE---AEAEAERII 98
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 111-209 3.91e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729728614 111 ESNNVErEFLQGAT-VADVAEGNEDIFglstDSLSHLRSpsVLEVREKGYERLKEELAKAQREAHKMVKEANVKQAAAEK 189
Cdd:COG3883  110 GSESFS-DFLDRLSaLSKIADADADLL----EELKADKA--ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182

                         90       100
                 ....*....|....*....|
gi 729728614 190 QLKEAQGKIDVLQAEVAALK 209
Cdd:COG3883  183 LLAQLSAEEAAAEAQLAELE 202
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 160-204 4.89e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.03  E-value: 4.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 729728614 160 ERLKEE----LAKAQREAHKMVKEANvKQAAAEKQ--LKEAQGKIDVLQAE 204
Cdd:cd06503   50 EELLAEyeekLAEARAEAQEIIEEAR-KEAEKIKEeiLAEAKEEAERILEQ 99
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 152-232 7.85e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.21  E-value: 7.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729728614 152 LEVREKGYERLKEELAKAQREAHKMVKEANVKQAAAEKQLKEAQGKIDVLQAEVAALKTLVLSTSPTSPTKEF-QSGGKT 230
Cdd:COG4942  176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFaALKGKL 255


                 ..
gi 729728614 231 PF 232
Cdd:COG4942  256 PW 257
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 155-208 8.61e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 36.26  E-value: 8.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 729728614 155 REKGYERLKEELAKAQREAHKMVKEANvKQAAAEKQlkEAqgkIDVLQAEVAAL 208
Cdd:cd06503   75 RKEAEKIKEEILAEAKEEAERILEQAK-AEIEQEKE--KA---LAELRKEVADL 122
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 152-212 8.86e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.60  E-value: 8.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 729728614 152 LEVREKgYERLKEELAKAQREAHKMVKEANVKQAAAEKQLKEAQGKIDVLQAEVAALKTLV 212
Cdd:COG1579  113 LELMER-IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
 
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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