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Conserved domains on  [gi|1035517627|ref|NP_001264301|]
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uncharacterized protein KIAA2012 isoform 1 [Homo sapiens]

Protein Classification

DUF4670 domain-containing protein( domain architecture ID 12174332)

DUF4670 domain-containing protein similar to Homo sapiens protein KIAA2012

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 624-1137 0e+00

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: 584.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  624 YETSPLTQTTEKQGAQQSLEAAAQKTGEPQSCINKALICSNRKEFYTRKLHIDMTPFLKESGNALDYQEEAGRPLRETHH 703
Cdd:pfam15709    1 KETSPLTQTTEEQGAQQSLEAAAQKTGEPQSCINKGLICSNRKEFYTRKLHIDMTPFLKDSGEALDSHEEPGEPLGENHQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  704 NDQDPEPRSMTLDSPRASRTEHIQTPEADIVQKV-GRDYDVHHLHRGLLGYGPESPERLSAVYTSLLPREREGKAEPRLF 782
Cdd:pfam15709   81 DSQDPEPRSVTLSPLSASLGEHIQTPEADTVQNGdGEDYDVHHLHRGLPRHRPESPEKLTAVDTSLLPRAREGKTEPRLF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  783 SQETSANISH-ERDLINEAKRKEKPKKDKTKGPKSEREGKVYGQAEAAIG-----KSKDSKAKKKLEKKTRPQRKRTQKE 856
Cdd:pfam15709  161 NQETPASISHaERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGksresKAEKKSELISKGKKTGAKRKRTQKE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  857 RNLEIAAELSGPDV-SYEETEDTSNRGSFASDSFVEDPWLSPKYDAQESQVSLDGRSSPSQIATVTGNMESKEERRCEDP 935
Cdd:pfam15709  241 RNLEVAAELSGPDViNSKETEDASERGAFSSDSVVEDPWLSSKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDP 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  936 SKALLTKREQEKASWDRLRAERAEMRWLEVEKKRREQEEQRQLQQEQLERAKKMEEELELEQQRRTEEIRLRKQRLQEEQ 1015
Cdd:pfam15709  321 SKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEER 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1016 QRQEEEERKQQLRLKAAQERARQQQEEFRRKLRELQRKKQQEEAERAEAEKQRQEELEMQLEEEQKHLMEMAEEERLEYQ 1095
Cdd:pfam15709  401 QRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQ 480

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1035517627 1096 RRKQEAEEKARLEAEERRQKEEEAARLALEEATKQAQEQARQ 1137
Cdd:pfam15709  481 RQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
 
Name Accession Description Interval E-value
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 624-1137 0e+00

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: 584.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  624 YETSPLTQTTEKQGAQQSLEAAAQKTGEPQSCINKALICSNRKEFYTRKLHIDMTPFLKESGNALDYQEEAGRPLRETHH 703
Cdd:pfam15709    1 KETSPLTQTTEEQGAQQSLEAAAQKTGEPQSCINKGLICSNRKEFYTRKLHIDMTPFLKDSGEALDSHEEPGEPLGENHQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  704 NDQDPEPRSMTLDSPRASRTEHIQTPEADIVQKV-GRDYDVHHLHRGLLGYGPESPERLSAVYTSLLPREREGKAEPRLF 782
Cdd:pfam15709   81 DSQDPEPRSVTLSPLSASLGEHIQTPEADTVQNGdGEDYDVHHLHRGLPRHRPESPEKLTAVDTSLLPRAREGKTEPRLF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  783 SQETSANISH-ERDLINEAKRKEKPKKDKTKGPKSEREGKVYGQAEAAIG-----KSKDSKAKKKLEKKTRPQRKRTQKE 856
Cdd:pfam15709  161 NQETPASISHaERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGksresKAEKKSELISKGKKTGAKRKRTQKE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  857 RNLEIAAELSGPDV-SYEETEDTSNRGSFASDSFVEDPWLSPKYDAQESQVSLDGRSSPSQIATVTGNMESKEERRCEDP 935
Cdd:pfam15709  241 RNLEVAAELSGPDViNSKETEDASERGAFSSDSVVEDPWLSSKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDP 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  936 SKALLTKREQEKASWDRLRAERAEMRWLEVEKKRREQEEQRQLQQEQLERAKKMEEELELEQQRRTEEIRLRKQRLQEEQ 1015
Cdd:pfam15709  321 SKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEER 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1016 QRQEEEERKQQLRLKAAQERARQQQEEFRRKLRELQRKKQQEEAERAEAEKQRQEELEMQLEEEQKHLMEMAEEERLEYQ 1095
Cdd:pfam15709  401 QRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQ 480

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1035517627 1096 RRKQEAEEKARLEAEERRQKEEEAARLALEEATKQAQEQARQ 1137
Cdd:pfam15709  481 RQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1031-1155 1.20e-10

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 64.83  E-value: 1.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1031 AAQERARQQQEEFRRKLRELQRKKQQEEAERAEAEKQrqeelemqlEEEQKHLMEMaEEERLEYQRRKQEAEEKARLEAE 1110
Cdd:PRK09510    60 VVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQ---------AAEQERLKQL-EKERLAAQEQKKQAEEAAKQAAL 129

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1035517627 1111 ERRQKEEEAARLA-------------LEEATKQAQEQARQKAALEKHFHFYQELHKEA 1155
Cdd:PRK09510   130 KQKQAEEAAAKAAaaakakaeaeakrAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKA 187
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1030-1142 1.38e-07

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: 54.85  E-value: 1.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1030 KAAQERARQQQEEFRRKLRELQRKKQQEEAERAEAEKQ-----RQEELEMQLEEEQKhlMEMAEEERLEY-QRRKQEAEE 1103
Cdd:TIGR02794   47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRaaeqaRQKELEQRAAAEKA--AKQAEQAAKQAeEKQKQAEEA 124

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1035517627 1104 KARLEAEERRQKEEEAARLALEEATKQAQEQARQKAALE 1142
Cdd:TIGR02794  125 KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAE 163
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1084-1158 1.80e-05

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: 45.51  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1084 MEMAEEERLEYQRRKQEAEEK---ARLEAEE-----RRQKEEEAARlALEEATKQAQ---EQARQKAALEKHfHFYQELH 1152
Cdd:cd06503     39 LEEAEKAKEEAEELLAEYEEKlaeARAEAQEiieeaRKEAEKIKEE-ILAEAKEEAErilEQAKAEIEQEKE-KALAELR 116


                   ....*.
gi 1035517627 1153 KEASGL 1158
Cdd:cd06503    117 KEVADL 122
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1031-1144 2.92e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 44.86  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1031 AAQERARQ-QQEEFRRKlRELQRKKQQEEAERAEAEKQRQEELEMQLEEEQKHLmEMAEEERLEyQRRKQEAEEKARLEA 1109
Cdd:COG2268    240 AEAEAELAkKKAEERRE-AETARAEAEAAYEIAEANAEREVQRQLEIAEREREI-ELQEKEAER-EEAELEADVRKPAEA 316

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1035517627 1110 EERRQKEEEAARL--ALEEATKQAQEQARQKAALEKH 1144
Cdd:COG2268    317 EKQAAEAEAEAEAeaIRAKGLAEAEGKRALAEAWNKL 353
 
Name Accession Description Interval E-value
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 624-1137 0e+00

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: 584.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  624 YETSPLTQTTEKQGAQQSLEAAAQKTGEPQSCINKALICSNRKEFYTRKLHIDMTPFLKESGNALDYQEEAGRPLRETHH 703
Cdd:pfam15709    1 KETSPLTQTTEEQGAQQSLEAAAQKTGEPQSCINKGLICSNRKEFYTRKLHIDMTPFLKDSGEALDSHEEPGEPLGENHQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  704 NDQDPEPRSMTLDSPRASRTEHIQTPEADIVQKV-GRDYDVHHLHRGLLGYGPESPERLSAVYTSLLPREREGKAEPRLF 782
Cdd:pfam15709   81 DSQDPEPRSVTLSPLSASLGEHIQTPEADTVQNGdGEDYDVHHLHRGLPRHRPESPEKLTAVDTSLLPRAREGKTEPRLF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  783 SQETSANISH-ERDLINEAKRKEKPKKDKTKGPKSEREGKVYGQAEAAIG-----KSKDSKAKKKLEKKTRPQRKRTQKE 856
Cdd:pfam15709  161 NQETPASISHaERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGksresKAEKKSELISKGKKTGAKRKRTQKE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  857 RNLEIAAELSGPDV-SYEETEDTSNRGSFASDSFVEDPWLSPKYDAQESQVSLDGRSSPSQIATVTGNMESKEERRCEDP 935
Cdd:pfam15709  241 RNLEVAAELSGPDViNSKETEDASERGAFSSDSVVEDPWLSSKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDP 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  936 SKALLTKREQEKASWDRLRAERAEMRWLEVEKKRREQEEQRQLQQEQLERAKKMEEELELEQQRRTEEIRLRKQRLQEEQ 1015
Cdd:pfam15709  321 SKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEER 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1016 QRQEEEERKQQLRLKAAQERARQQQEEFRRKLRELQRKKQQEEAERAEAEKQRQEELEMQLEEEQKHLMEMAEEERLEYQ 1095
Cdd:pfam15709  401 QRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQ 480

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1035517627 1096 RRKQEAEEKARLEAEERRQKEEEAARLALEEATKQAQEQARQ 1137
Cdd:pfam15709  481 RQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1031-1155 1.20e-10

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 64.83  E-value: 1.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1031 AAQERARQQQEEFRRKLRELQRKKQQEEAERAEAEKQrqeelemqlEEEQKHLMEMaEEERLEYQRRKQEAEEKARLEAE 1110
Cdd:PRK09510    60 VVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQ---------AAEQERLKQL-EKERLAAQEQKKQAEEAAKQAAL 129

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1035517627 1111 ERRQKEEEAARLA-------------LEEATKQAQEQARQKAALEKHFHFYQELHKEA 1155
Cdd:PRK09510   130 KQKQAEEAAAKAAaaakakaeaeakrAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKA 187
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1030-1142 1.36e-10

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 64.83  E-value: 1.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1030 KAAQERARQQQEEfRRKLRELQRKKQQEEAERAEAEKQRQEELEMQLEEEQKHLMEMAEEERLEYQRRKQEAEEKARLEA 1109
Cdd:PRK09510    95 KQAAEQERLKQLE-KERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEA 173

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1035517627 1110 EERRQKEEEAARLALEEATKQAQEQARQKAALE 1142
Cdd:PRK09510   174 EAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAE 206
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1030-1142 1.38e-07

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: 54.85  E-value: 1.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1030 KAAQERARQQQEEFRRKLRELQRKKQQEEAERAEAEKQ-----RQEELEMQLEEEQKhlMEMAEEERLEY-QRRKQEAEE 1103
Cdd:TIGR02794   47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRaaeqaRQKELEQRAAAEKA--AKQAEQAAKQAeEKQKQAEEA 124

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1035517627 1104 KARLEAEERRQKEEEAARLALEEATKQAQEQARQKAALE 1142
Cdd:TIGR02794  125 KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAE 163
PTZ00121 PTZ00121
MAEBL; Provisional
 925-1143 1.12e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  925 ESKEERRCEDPSKALLTKREQEKASWDRLRAEraEMRWLEVEKKRREQEEQRQLQQEQLERAKKMEEELELEQQRRTEEI 1004
Cdd:PTZ00121  1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAE--EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1005 RLRKQRLQEEQQRQEeeerkqqlrlKAAQERARQQQEEFRRKLRELQRKKQQEeaeraeaeKQRQEELEMQLEEEQK--- 1081
Cdd:PTZ00121  1631 EKKKVEQLKKKEAEE----------KKKAEELKKAEEENKIKAAEEAKKAEED--------KKKAEEAKKAEEDEKKaae 1692

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1035517627 1082 HLMEMAEEERLEYQRRKQEAEEKARleAEERRqKEEEAARLALEEATKQAQEQARQKAALEK 1143
Cdd:PTZ00121  1693 ALKKEAEEAKKAEELKKKEAEEKKK--AEELK-KAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
Radial_spoke_3 pfam06098
Radial spoke protein 3; This family consists of several radial spoke protein 3 (RSP3) ...
 1083-1140 3.35e-06

Radial spoke protein 3; This family consists of several radial spoke protein 3 (RSP3) sequences. Eukaryotic cilia and flagella present in diverse types of cells perform motile, sensory, and developmental functions in organizms from protists to humans. They are centred by precisely organized, microtubule-based structures, the axonemes. The axoneme consists of two central singlet microtubules, called the central pair, and nine outer doublet microtubules. These structures are well-conserved during evolution. The outer doublet microtubules, each composed of A and B sub-fibres, are connected to each other by nexin links, while the central pair is held at the centre of the axoneme by radial spokes. The radial spokes are T-shaped structures extending from the A-tubule of each outer doublet microtubule to the centre of the axoneme. Radial spoke protein 3 (RSP3), is present at the proximal end of the spoke stalk and helps in anchoring the radial spoke to the outer doublet. It is thought that radial spokes regulate the activity of inner arm dynein through protein phosphorylation and dephosphorylation.


Pssm-ID: 461827  Cd Length: 286  Bit Score: 50.33  E-value: 3.35e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1035517627 1083 LMEMAEEERLEYQRRKQEA------EEKA---RLEAEERRQKEEEAARLALEEATKQAQEQARQKAA 1140
Cdd:pfam06098  146 LLEVLEEEELANLREQQRAfeelrnAELAevqRLEEQERRLREEKERRIAQQREALKKEKETAEKIA 212
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
 1097-1156 1.05e-05

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: 47.74  E-value: 1.05e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1097 RKQEAEEKARLEAEERRQKEEEAARLALEEATKQAQEQARQKAALEKHFHFYQELHKEAS 1156
Cdd:pfam15927    1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELEELKHLLEERKEALE 60
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1084-1158 1.80e-05

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: 45.51  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1084 MEMAEEERLEYQRRKQEAEEK---ARLEAEE-----RRQKEEEAARlALEEATKQAQ---EQARQKAALEKHfHFYQELH 1152
Cdd:cd06503     39 LEEAEKAKEEAEELLAEYEEKlaeARAEAQEiieeaRKEAEKIKEE-ILAEAKEEAErilEQAKAEIEQEKE-KALAELR 116


                   ....*.
gi 1035517627 1153 KEASGL 1158
Cdd:cd06503    117 KEVADL 122
PTZ00121 PTZ00121
MAEBL; Provisional
 927-1143 2.54e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 2.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  927 KEERRCEDPSKALLTKREQEkASWDRLRAERAE-MRWLEVEKKRREQEEQRQLQQEQLERA---KKMEEELELEQQRRTE 1002
Cdd:PTZ00121  1215 EEARKAEDAKKAEAVKKAEE-AKKDAEEAKKAEeERNNEEIRKFEEARMAHFARRQAAIKAeeaRKADELKKAEEKKKAD 1293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1003 EIRLRKQRLQEEQQRQEEEERKQQLRLKAAQERARQQQEEFRRKLRELQRKKQQEEAERAEAEKQRQEELEMQLEEEQKh 1082
Cdd:PTZ00121  1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK- 1372

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1035517627 1083 lmemAEEERLEYQRRKQEAEEKARLE-----AEERRQKEEE-----AARLALEEATKQAQEQARQKAALEK 1143
Cdd:PTZ00121  1373 ----KEEAKKKADAAKKKAEEKKKADeakkkAEEDKKKADElkkaaAAKKKADEAKKKAEEKKKADEAKKK 1439
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1006-1143 1.01e-04

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: 45.99  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1006 LRKQRLqeeqqrqeeeerkqqlrlkaaQERARQQQEEFRRKLRELQRKKQQEEAERAEAEKQrqeelemqleeeqkhlme 1085
Cdd:TIGR02794   80 AEKQRA---------------------AEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQ------------------ 120

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1035517627 1086 mAEEerleyQRRKQEAEEKARLEAEERRQKEEEAARLALEEATKQAQEQARQKAALEK 1143
Cdd:TIGR02794  121 -AEE-----AKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK 172
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1034-1137 1.02e-04

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: 46.66  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1034 ERARQQQEEFRRKLRELQRKKQQEEAERAEAEK-----QRQEELEMQLEEEQKHLMEMAEEERL-----EYQRRKQEAEE 1103
Cdd:pfam17380  463 ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKilekeLEERKQAMIEEERKRKLLEKEMEERQkaiyeEERRREAEEER 542

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1035517627 1104 KARLEAEERRQKEEEAARLALEEATKQAQEQARQ 1137
Cdd:pfam17380  543 RKQQEMEERRRIQEQMRKATEERSRLEAMERERE 576
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1033-1137 2.73e-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: 42.72  E-value: 2.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1033 QERARQQQEEFRRKLRELQRKKQQEEAERAEAEKQRQEELEMQLEEEQKHLmemAEEERLEyqRRKQEAEEKARLEaeer 1112
Cdd:pfam05672   30 EEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRK---AEEEAEE--REQREQEEQERLQ---- 100

                           90       100
                   ....*....|....*....|....*
gi 1035517627 1113 RQKEEEAARlALEEATKQAQEQARQ 1137
Cdd:pfam05672  101 KQKEEAEAK-AREEAERQRQEREKI 124
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
1031-1144 2.92e-04

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 44.86  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1031 AAQERARQ-QQEEFRRKlRELQRKKQQEEAERAEAEKQRQEELEMQLEEEQKHLmEMAEEERLEyQRRKQEAEEKARLEA 1109
Cdd:COG2268    240 AEAEAELAkKKAEERRE-AETARAEAEAAYEIAEANAEREVQRQLEIAEREREI-ELQEKEAER-EEAELEADVRKPAEA 316

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1035517627 1110 EERRQKEEEAARL--ALEEATKQAQEQARQKAALEKH 1144
Cdd:COG2268    317 EKQAAEAEAEAEAeaIRAKGLAEAEGKRALAEAWNKL 353
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 1028-1133 3.38e-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: 3.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1028 RLKAAQE---RARQQQEEFRRKLRELQRKKQQEEAERAEAEKQRQEELEMQLEEEQKHLMEMAEEERLEyqRRKQEAEEK 1104
Cdd:pfam20492   14 RLKQYEEetkKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLE--AELAEAQEE 91

                           90       100
                   ....*....|....*....|....*....
gi 1035517627 1105 ARLEAEERRQKEEEAARlaLEEATKQAQE 1133
Cdd:pfam20492   92 IARLEEEVERKEEEARR--LQEELEEARE 118
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1033-1144 4.56e-04

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: 43.75  E-value: 4.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1033 QERARQQQEEFRRKLRELQRKKQQEEAERAEAEKQRQEELEMQleeeqKHLMEMAEEERLEYQRRKQEAEEKARLEAEE- 1111
Cdd:pfam13868  104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELE-----KEEEREEDERILEYLKEKAEREEEREAEREEi 178

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1035517627 1112 RRQKEEEAARLA----LEEATKQAQEQARQKAALEKH 1144
Cdd:pfam13868  179 EEEKEREIARLRaqqeKAQDEKAERDELRAKLYQEEQ 215
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 1028-1155 6.03e-04

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: 43.37  E-value: 6.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1028 RLKAAQERARQQ--QEEFRRKLRELQRKKQQEEAERAEAEKQRQEELEMQLEEEQKHLMEMAEEERLEYQRRKQEAEEKA 1105
Cdd:pfam13868  198 DEKAERDELRAKlyQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE 277

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1035517627 1106 RLEAEERRQKEEEAARlaleEATKQAQEQARQKAA-LEKHFHFYQELHKEA 1155
Cdd:pfam13868  278 QEEAEKRRMKRLEHRR----ELEKQIEEREEQRAAeREEELEEGERLREEE 324
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1002-1143 6.64e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 6.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1002 EEIRLRKQRLQEEQQRQEEEErkQQLRLKAAQERARQQQEEFRRKLRELQRKKQQEEAERAEAEKQRQEELEMQLEEEQK 1081
Cdd:COG1196    296 ELARLEQDIARLEERRRELEE--RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1035517627 1082 HLMEMAEEERLEYQR---RKQEAEEKARLEAEERRQKEEEAARLALEEATKQAQEQARQKAALEK 1143
Cdd:COG1196    374 LAEAEEELEELAEELleaLRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
PRK12704 PRK12704
phosphodiesterase; Provisional
 1029-1155 6.82e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 6.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1029 LKAAQERARQQQEEFRRKLRELQRKKQQeeaeraeaekqrqeelemqleeeqkhlmemAEEERLEYQRRKQEAEEKARlE 1108
Cdd:PRK12704    84 LQKLEKRLLQKEENLDRKLELLEKREEE------------------------------LEKKEKELEQKQQELEKKEE-E 132

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1035517627 1109 AEERRQKE----EEAARLALEEATKQAQEQARQKAALEKhFHFYQELHKEA 1155
Cdd:PRK12704   133 LEELIEEQlqelERISGLTAEEAKEILLEKVEEEARHEA-AVLIKEIEEEA 182
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 1030-1140 6.92e-04

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: 41.31  E-value: 6.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1030 KAAQERARQQQEEFRRKLRELQRKKQqeeaeraeaekqrqeelemqleeeqkhlmEMAEEERLEYQRRKQEAEEKARLEA 1109
Cdd:COG0711     44 ERAKEEAEAALAEYEEKLAEARAEAA-----------------------------EIIAEARKEAEAIAEEAKAEAEAEA 94

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1035517627 1110 EERRqkeeEAARLALEEATKQAQEQARQKAA 1140
Cdd:COG0711     95 ERII----AQAEAEIEQERAKALAELRAEVA 121
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 1030-1143 7.55e-04

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: 43.30  E-value: 7.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1030 KAAQERARQQQEEFRRKLRELQRKKQQEEAERAEAE--KQRQEELEMQLEEEQKHLMEMAEEERLEYQRRKQEAEEKARl 1107
Cdd:TIGR02794  112 KQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEaaKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAK- 190

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1035517627 1108 eAEERRQKEEEAARLALEEATKQAQEQARQKAALEK 1143
Cdd:TIGR02794  191 -AEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEA 225
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1084-1155 8.45e-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: 41.18  E-value: 8.45e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1035517627 1084 MEMAEEERLEY-QRRKQEAEEKARLEAEERRQKEEEaaRLALEEATKQAQEQARQKAALEKHFHFYQELHKEA 1155
Cdd:pfam05672   35 LEKEEEERLRKeELRRRAEEERARREEEARRLEEER--RREEEERQRKAEEEAEEREQREQEEQERLQKQKEE 105
PTZ00121 PTZ00121
MAEBL; Provisional
 925-1143 9.78e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 9.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  925 ESKEERRCEDPSKALLTKREQEKASwdrlRAERAEMRWLEVEKKRREQEEQRQLQQEQLERAKKMEEELELEQQRRTEEI 1004
Cdd:PTZ00121  1291 KADEAKKAEEKKKADEAKKKAEEAK----KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1005 RLRKQRLQEEQQRQEEEERKQQLRLKAaqERARQQQEEFRRKLRELQR----KKQQEEAERAEAEKQRQEELEMQLEEEQ 1080
Cdd:PTZ00121  1367 EAAEKKKEEAKKKADAAKKKAEEKKKA--DEAKKKAEEDKKKADELKKaaaaKKKADEAKKKAEEKKKADEAKKKAEEAK 1444

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1035517627 1081 K--HLMEMAEEERlEYQRRKQEAEEKARleAEERRQKEEEAARlaLEEATKQAQEQARQKAALEK 1143
Cdd:PTZ00121  1445 KadEAKKKAEEAK-KAEEAKKKAEEAKK--ADEAKKKAEEAKK--ADEAKKKAEEAKKKADEAKK 1504
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1028-1159 1.20e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1028 RLKAAQERARQQQEEFRRKLRELQRKKQQEEAERAEAEKQRQEELEMQLEEEQKHLmemAEEERLEYQRRKQEAEEKARL 1107
Cdd:COG1196    271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA---ELEEELEELEEELEELEEELE 347

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1035517627 1108 EAEERR----QKEEEAARLALEEATKQAQEQARQKAALEKHFHFYQELHKEASGLQ 1159
Cdd:COG1196    348 EAEEELeeaeAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1002-1143 1.25e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1002 EEIRLRKQRLQEEQQRQEEEERKQQLRLKAAQERARQQQEEFRRKLRELQRKKQQEEAERAEAEKQ--RQEELEMQLEEE 1079
Cdd:COG1196    351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLerLEEELEELEEAL 430

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1035517627 1080 QKHLMEMAEEERLEYQRRKQEAEEKARLEAEERRQKEEEAARLALEEATKQAQEQARQKAALEK 1143
Cdd:COG1196    431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 1029-1143 1.48e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.85  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1029 LKAAQERarqqQEEFRRKLRELQRKKQQEEAERAEAEKQrqeelemqlEEEQKHLMEMAEEERLEYQRRKQEAEE----- 1103
Cdd:pfam01576   14 LQKVKER----QQKAESELKELEKKHQQLCEEKNALQEQ---------LQAETELCAEAEEMRARLAARKQELEEilhel 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1035517627 1104 KARLEAEERR------QKEEEAARLALEEATKQAQEQARQKAALEK 1143
Cdd:pfam01576   81 ESRLEEEEERsqqlqnEKKKMQQHIQDLEEQLDEEEAARQKLQLEK 126
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 916-1143 2.23e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  916 QIATVTGNMESKEERRcedpsKALLTKREQEKASWDRLRAERAEMR---------WLEVEKKRREQEEQRQLQQEQLERA 986
Cdd:COG1196    240 ELEELEAELEELEAEL-----EELEAELAELEAELEELRLELEELEleleeaqaeEYELLAELARLEQDIARLEERRREL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  987 KKMEEELELEQQRRTEEIRLRKqrlqeeqqRQEEEERKQQLRLKAAQERARQQQEEFRRKLRELQRKKQQEEAERAEAEK 1066
Cdd:COG1196    315 EERLEELEEELAELEEELEELE--------EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1035517627 1067 QRQEELEMQLEEEQKHLMEMAEEERLEYQRRKQEAEEKARLEAEERRQKEEEAARLALEEATKQAQEQARQKAALEK 1143
Cdd:COG1196    387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 1030-1140 2.40e-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: 39.34  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1030 KAAQERARQQQEEFRRKLRELQRKkqqeeaeraeaekqrqeelemqleeeqkhlmemAEEERLEYQRRKQEAEEKARLEA 1109
Cdd:cd06503     43 EKAKEEAEELLAEYEEKLAEARAE---------------------------------AQEIIEEARKEAEKIKEEILAEA 89

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1035517627 1110 EERRQKEEEAARLALEEATKQAQEQARQKAA 1140
Cdd:cd06503     90 KEEAERILEQAKAEIEQEKEKALAELRKEVA 120
PTZ00121 PTZ00121
MAEBL; Provisional
 925-1143 2.78e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 2.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  925 ESKEERRCEDpskalLTKREQEKASWDRLRAERAEMRWLEVEKKRREQEEQRQLQQEQLERAKKMEEE-LELEQQRRTEE 1003
Cdd:PTZ00121  1452 KAEEAKKAEE-----AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEAKKADE 1526

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1004 IR----------LRKQRLQEEQQRQEEEERKQQLRLKAAQERARQQQEEFRRKLRELQRKKQQEEAERAEAEKQRQEELE 1073
Cdd:PTZ00121  1527 AKkaeeakkadeAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1074 MQLEEEQKhlmemAEEERLEYQRRKQEAEEKARL------EAEERRQ-----KEEEAARLALEEATKQAQEQARQKAALE 1142
Cdd:PTZ00121  1607 MKAEEAKK-----AEEAKIKAEELKKAEEEKKKVeqlkkkEAEEKKKaeelkKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681


                   .
gi 1035517627 1143 K 1143
Cdd:PTZ00121  1682 K 1682
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1030-1140 3.27e-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: 3.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1030 KAAQERARQQQEEFRRKLRELQRKKQQEEAERAEAEKQRQEELEMQLEEEQKHLMEMAEEERLEYQRRKQEAEEKARLEA 1109
Cdd:COG1196    398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1035517627 1110 EERRQKEEEAARLALEEATKQAQEQARQKAA 1140
Cdd:COG1196    478 ALAELLEELAEAAARLLLLLEAEADYEGFLE 508
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 1031-1138 3.41e-03

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 40.46  E-value: 3.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1031 AAQERARQQQEEFRRKLRE-------LQRKKQQEEAERAEAEKQRQEELEMQLEEEQKH--LMEMAEEERLEYQRRKQEA 1101
Cdd:pfam13904   75 QKEEREKEEQEAELRKRLAkekyqewLQRKARQQTKKREESHKQKAAESASKSLAKPERkvSQEEAKEVLQEWERKKLEQ 154

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1035517627 1102 EEKARLEAEERRQKEEEaarlaLEEATKQAQEQARQK 1138
Cdd:pfam13904  155 QQRKREEEQREQLKKEE-----EEQERKQLAEKAWQK 186
PTZ00121 PTZ00121
MAEBL; Provisional
 925-1143 3.80e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 3.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627  925 ESKEERRCEDPSKalltKREQEKASWDRLR-AERAEMRWLEVEKKRREQEEQRQLQQEQLERA---KKMEEELELEQQRR 1000
Cdd:PTZ00121  1478 KAEEAKKADEAKK----KAEEAKKKADEAKkAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeaKKAEEKKKADELKK 1553

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1001 TEEIRLRKQRLQEEQQRQEEEERKQQLRLKAAQERARQQQEEFRRKLRELQR--KKQQEEAERAEAEKQRQEELEMQLEE 1078
Cdd:PTZ00121  1554 AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKkmKAEEAKKAEEAKIKAEELKKAEEEKK 1633

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1035517627 1079 EQKHLMEMAEEERLEYQRRKQEaEEKARLEAEERRQKEEEAARLAlEEATKQAQEQARQKAALEK 1143
Cdd:PTZ00121  1634 KVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAKKAEEDKKKA-EEAKKAEEDEKKAAEALKK 1696
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1030-1119 3.85e-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: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1030 KAAQERARQQQEEFRRKLRELQRKKQQeeaeraeaeKQRQEELEMQLEEEQKHLMEMAEEERLEYQRRKQEAEEKARLEA 1109
Cdd:pfam05672   51 RAEEERARREEEARRLEEERRREEEER---------QRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQER 121

                           90
                   ....*....|
gi 1035517627 1110 EERRQKEEEA 1119
Cdd:pfam05672  122 EKIMQQEEQE 131
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1026-1145 5.19e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 5.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1026 QLRLKAAQERARQQQEEFRRKLRELQRKKQ--QEEAERAEAEKQRQEELEMQLEEEQKHL---MEMAEEERLEYQRRKQE 1100
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVSELEEEIEelQKELYALANEISRLEQQKQILRERLANLerqLEELEAQLEELESKLDE 334

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1035517627 1101 -AEEKARLEAEERRQKEE-EAARLALEEATKQAQEQARQKAALEKHF 1145
Cdd:TIGR02168  335 lAEELAELEEKLEELKEElESLEAELEELEAELEELESRLEELEEQL 381
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1028-1140 5.45e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.79  E-value: 5.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1028 RLKAAQERARQQQEEFRRKLRELQRKKQQEEAERAEAEKQRQEELEMQLEEEQKHLMEMAEEERLEYQRRKQEAEEKARL 1107
Cdd:COG3064     31 AEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAA 110

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1035517627 1108 E---AEERRQKEEEAARLALEEATKQAQEQARQKAA 1140
Cdd:COG3064    111 EkaaAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEA 146
PLN02316 PLN02316
synthase/transferase
 1086-1156 7.55e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 40.62  E-value: 7.55e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1035517627 1086 MAEEERLEYQRRKQEAEEKARLEAEERRQKEEEAARLAleeatkqaqEQARQKAALEKHFHFYQELHKEAS 1156
Cdd:PLN02316   250 LLEEKRRELEKLAKEEAERERQAEEQRRREEEKAAMEA---------DRAQAKAEVEKRREKLQNLLKKAS 311
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 1034-1145 9.18e-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: 9.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1034 ERARQQQEEFRRKLRElqrKKQQEEAERAEAEKQ-RQEELEMQLEEEQKHLMEMAEEERLEYQRRKQEAEE--KARLEAE 1110
Cdd:pfam05672   10 EEAARILAEKRRQARE---QREREEQERLEKEEEeRLRKEELRRRAEEERARREEEARRLEEERRREEEERqrKAEEEAE 86

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1035517627 1111 ERRQKE-EEAARLAL--EEATKQAQEQA-RQKAALEKHF 1145
Cdd:pfam05672   87 EREQREqEEQERLQKqkEEAEAKAREEAeRQRQEREKIM 125
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
 1085-1151 9.55e-03

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 38.24  E-value: 9.55e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1035517627 1085 EMAEEERLeyqrRKQEAEEKARLEAEERRQKEEEAARLALEEATKQAQEQARQKAALEKHFHFYQEL 1151
Cdd:pfam15236   83 EQEEEERL----RREREEEQKQFEEERRKQKEKEEAMTRKTQALLQAMQKAQELAQRLKQEQRIREL 145
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1034-1159 9.80e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 9.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1034 ERARQQQEEFRRKLRELQ------RKKQQEEAERAEAEKQRQEELEMQLEEEQKHLMEMAEEERLEYQRRKQEAEEKARL 1107
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEkalaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1035517627 1108 EAE-----ERRQKEEEAARLALEEATKQAQEQARQKAALEKHFHFYQELHKEASGLQ 1159
Cdd:TIGR02168  760 EAEieeleERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 1044-1153 9.93e-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: 38.48  E-value: 9.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035517627 1044 RRKLRELQRKKQQEEAERAEAEKQRqeelemqlEEEQKHLMEMAEEERLEYQRRKQEAEEKARLEAEERRQKEEEAARLA 1123
Cdd:pfam09756    8 RAKLELKEAKRQQREAEEEEREERE--------KLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQEEYEKLK 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1035517627 1124 LEEATKQ---AQEQARQKAALEKHFHFYQELHK 1153
Cdd:pfam09756   80 SQFVVEEegtDKLSAEDESQLLEDFINYIKLKK 112
 
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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