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Conserved domains on  [gi|1958748278|ref|XP_038954166|]
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hydrocephalus-inducing protein homolog isoform X5 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Hydin_ADK pfam17213
Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to ...
1082-1306 5.54e-104

Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to adenylate kinases.


:

Pssm-ID: 465383  Cd Length: 199  Bit Score: 332.10  E-value: 5.54e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1082 AIIVYGTPVSGKTANAISMAKFYNTACLNIDSIVLEALSDSNNVLGIRARELCIRAAIEQSMREAEESAQESSVTQNLGA 1161
Cdd:pfam17213    1 AIIVHGAPLSGKTATAVTLAKHYGAACLTIDSIVLEAISDGNSIAGLRARELCARAAIEQSEREAEEAAQEAAVVPGQPT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1162 PARLSTENLGRFTSDLTLLTQEYKIPKSMRGSVMLSKGKTESHWSGSqkqqgqqqqqqqqqqpqqqqqpqqqqQQQHHQH 1241
Cdd:pfam17213   81 TYRLSVEALTKHTSEGTLVGPESKISKGKRGSVVSGKGKADSHGTGS--------------------------QKQHHQH 134
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958748278 1242 QSETPQISSSPLLGGPTQRRLSVSASIGGETGLMSCVLPDDLLIQILAERIQLSDCFRGVVFDGL 1306
Cdd:pfam17213  135 QSETPQISSSPPPAGPIQRRLSVSASVGGEEGLMSCVLPEDLLVEILAERIQLNDCHRGVVFDGL 199
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
1344-1491 3.20e-12

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


The actual alignment was detected with superfamily member pfam17380:

Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 73.23  E-value: 3.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQaLRERKKRELERLAREMHEKKLQQELERQ 1423
Cdd:pfam17380  389 QKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR-LEEERAREMERVRLEEQERQQQVERLRQ 467
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958748278 1424 KEEDELKRKVKRPKPGPVAKEEPPLKK----SQGPTNKQlpSVAKLEMKMESIERKVSVREHGLLEETTRKK 1491
Cdd:pfam17380  468 QEEERKRKKLELEKEKRDRKRAEEQRRkileKELEERKQ--AMIEEERKRKLLEKEMEERQKAIYEEERRRE 537
Adk super family cl33950
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
1280-1336 6.65e-04

Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


The actual alignment was detected with superfamily member COG0563:

Pssm-ID: 440329 [Multi-domain]  Cd Length: 212  Bit Score: 43.96  E-value: 6.65e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1280 PDDLLIQILAERIQLSDCFRGVVFDGldtlFARNAPSALIclLKAIGSREHI---YVINM 1336
Cdd:COG0563     60 PDEIVIGLVKERLAQPDCANGFILDG----FPRTVAQAEA--LDELLAELGIkldAVIEL 113
 
Name Accession Description Interval E-value
Hydin_ADK pfam17213
Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to ...
1082-1306 5.54e-104

Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to adenylate kinases.


Pssm-ID: 465383  Cd Length: 199  Bit Score: 332.10  E-value: 5.54e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1082 AIIVYGTPVSGKTANAISMAKFYNTACLNIDSIVLEALSDSNNVLGIRARELCIRAAIEQSMREAEESAQESSVTQNLGA 1161
Cdd:pfam17213    1 AIIVHGAPLSGKTATAVTLAKHYGAACLTIDSIVLEAISDGNSIAGLRARELCARAAIEQSEREAEEAAQEAAVVPGQPT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1162 PARLSTENLGRFTSDLTLLTQEYKIPKSMRGSVMLSKGKTESHWSGSqkqqgqqqqqqqqqqpqqqqqpqqqqQQQHHQH 1241
Cdd:pfam17213   81 TYRLSVEALTKHTSEGTLVGPESKISKGKRGSVVSGKGKADSHGTGS--------------------------QKQHHQH 134
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958748278 1242 QSETPQISSSPLLGGPTQRRLSVSASIGGETGLMSCVLPDDLLIQILAERIQLSDCFRGVVFDGL 1306
Cdd:pfam17213  135 QSETPQISSSPPPAGPIQRRLSVSASVGGEEGLMSCVLPEDLLVEILAERIQLNDCHRGVVFDGL 199
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
1344-1491 3.20e-12

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: 73.23  E-value: 3.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQaLRERKKRELERLAREMHEKKLQQELERQ 1423
Cdd:pfam17380  389 QKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR-LEEERAREMERVRLEEQERQQQVERLRQ 467
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958748278 1424 KEEDELKRKVKRPKPGPVAKEEPPLKK----SQGPTNKQlpSVAKLEMKMESIERKVSVREHGLLEETTRKK 1491
Cdd:pfam17380  468 QEEERKRKKLELEKEKRDRKRAEEQRRkileKELEERKQ--AMIEEERKRKLLEKEMEERQKAIYEEERRRE 537
PTZ00121 PTZ00121
MAEBL; Provisional
1322-1491 1.00e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 1.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1322 LKAIGSREHIYVINMSQDYVAMKAqEKAKKELEETKRQEALAKEkerlqtldeEEYDALTAEQKIAFDREVRQAlRERKK 1401
Cdd:PTZ00121  1586 AKKAEEARIEEVMKLYEEEKKMKA-EEAKKAEEAKIKAEELKKA---------EEEKKKVEQLKKKEAEEKKKA-EELKK 1654
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1402 RELERLAREMHEKKLQQELERQKEEDELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLE-MKMESIERKVSVRE 1480
Cdd:PTZ00121  1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEeLKKAEEENKIKAEE 1734
                          170
                   ....*....|.
gi 1958748278 1481 HGLLEETTRKK 1491
Cdd:PTZ00121  1735 AKKEAEEDKKK 1745
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
1344-1527 2.84e-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: 56.01  E-value: 2.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKKELEETKRQ--EALAKEKERLQTLDE---EEYDALTAEQ--KIAFDREvRQALRERKKRELERLARE--MHEK 1414
Cdd:TIGR02794   64 KKEQERQKKLEQQAEEaeKQRAAEQARQKELEQraaAEKAAKQAEQaaKQAEEKQ-KQAEEAKAKQAAEAKAKAeaEAER 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1415 KLQQELERQKEED-------ELKRKV----KRPKPGPVAKEEpPLKKSQGPTNKQLPSVAKLEMKMESIERKvsVREHGL 1483
Cdd:TIGR02794  143 KAKEEAAKQAEEEakakaaaEAKKKAeeakKKAEAEAKAKAE-AEAKAKAEEAKAKAEAAKAKAAAEAAAKA--EAEAAA 219
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1484 LEETTRKKKATTEYAFGFP------ITQEQEESEGDFLKDSDKNLAQKFK 1527
Cdd:TIGR02794  220 AAAAEAERKADEAELGDIFglasgsNAEKQGGARGAAAGSEVDKYAAIIQ 269
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1345-1493 3.29e-07

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 56.20  E-value: 3.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1345 AQEKAKKELEETKRQEALAKEKERLQTLDEEEYDAL--TAEQKIAFDREVRQALRE--RKKRELERLAREMHEKKLQQEL 1420
Cdd:COG3064      1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKeeAEEERLAELEAKRQAEEEarEAKAEAEQRAAELAAEAAKKLA 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958748278 1421 ERQKEEDELKRKVKRPKPGPVAKEEPPLKKsqgptnKQLPSVAKLEmKMESIERKVsvrehglleETTRKKKA 1493
Cdd:COG3064     81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAA------EKAAAAAEKE-KAEEAKRKA---------EEEAKRKA 137
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
1331-1445 1.33e-06

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 50.66  E-value: 1.33e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278  1331 IYVINMSQDYVAMKAQEKAKKELEET--KRQEALAKEKERLQTLdEEEYDA----LTAEQkiafdREVRQALRERKKREL 1404
Cdd:smart00935    1 IGVVDVQKILQESPAGKAAQKQLEKEfkKRQAELEKLEKELQKL-KEKLQKdaatLSEAA-----REKKEKELQKKVQEF 74
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1958748278  1405 ERLAREMHEK--KLQQElERQKEEDELKRKVKRpkpgpVAKEE 1445
Cdd:smart00935   75 QRKQQKLQQDlqKRQQE-ELQKILDKINKAIKE-----VAKKK 111
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
1342-1435 2.51e-06

Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar proteins; mS26, also known as mitochondrial 37S ribosomal protein PET12, is a component of the mitochondrial small ribosomal subunit (mt-SSU) of Saccharomyces cerevisiae mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. The family also includes a group of uncharacterized proteins from pezizomycotina, which show high sequence similarity with mS26.


Pssm-ID: 467916 [Multi-domain]  Cd Length: 179  Bit Score: 50.63  E-value: 2.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1342 AMKAQEKAKKELEETKRQ---EALAKEKERLQTLDEEEydaltaEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQ 1418
Cdd:cd23703     44 PLSEYQEWKRKMAELRRQnlrEGLRELEERKLKTEELR------AKRSERKQAERERALNAPEREDERLTLPTIESALLG 117
                           90       100
                   ....*....|....*....|..
gi 1958748278 1419 ELERQ-----KEEDELKRKVKR 1435
Cdd:cd23703    118 PLMRVrtdpeREERAAKRRANR 139
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
1344-1454 9.02e-05

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 48.86  E-value: 9.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKKELEETKRQ--------------EALAKEKERLQTLDEEEYDALTAEQKIafdrEVRQALRERKKRELERLAR 1409
Cdd:NF033838   315 EAKKKAKDQKEEDRRNyptntyktleleiaESDVKVKEAELELVKEEAKEPRNEEKI----KQAKAKVESKKAEATRLEK 390
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958748278 1410 EMHEKKLQQELERQK--EEDELKRK-VKRPKPGPVAKEEPPLKKSQGP 1454
Cdd:NF033838   391 IKTDRKKAEEEAKRKaaEEDKVKEKpAEQPQPAPAPQPEKPAPKPEKP 438
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
1280-1336 6.65e-04

Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440329 [Multi-domain]  Cd Length: 212  Bit Score: 43.96  E-value: 6.65e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1280 PDDLLIQILAERIQLSDCFRGVVFDGldtlFARNAPSALIclLKAIGSREHI---YVINM 1336
Cdd:COG0563     60 PDEIVIGLVKERLAQPDCANGFILDG----FPRTVAQAEA--LDELLAELGIkldAVIEL 113
adk PRK00279
adenylate kinase; Reviewed
1280-1336 1.82e-03

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 42.83  E-value: 1.82e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958748278 1280 PDDLLIQILAERIQLSDCFRGVVFDGldtlFARNAP--SALICLLKAIGsREHIYVINM 1336
Cdd:PRK00279    60 PDEIVIGLVKERLAQPDCKNGFLLDG----FPRTIPqaEALDEMLKELG-IKLDAVIEI 113
 
Name Accession Description Interval E-value
Hydin_ADK pfam17213
Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to ...
1082-1306 5.54e-104

Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to adenylate kinases.


Pssm-ID: 465383  Cd Length: 199  Bit Score: 332.10  E-value: 5.54e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1082 AIIVYGTPVSGKTANAISMAKFYNTACLNIDSIVLEALSDSNNVLGIRARELCIRAAIEQSMREAEESAQESSVTQNLGA 1161
Cdd:pfam17213    1 AIIVHGAPLSGKTATAVTLAKHYGAACLTIDSIVLEAISDGNSIAGLRARELCARAAIEQSEREAEEAAQEAAVVPGQPT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1162 PARLSTENLGRFTSDLTLLTQEYKIPKSMRGSVMLSKGKTESHWSGSqkqqgqqqqqqqqqqpqqqqqpqqqqQQQHHQH 1241
Cdd:pfam17213   81 TYRLSVEALTKHTSEGTLVGPESKISKGKRGSVVSGKGKADSHGTGS--------------------------QKQHHQH 134
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958748278 1242 QSETPQISSSPLLGGPTQRRLSVSASIGGETGLMSCVLPDDLLIQILAERIQLSDCFRGVVFDGL 1306
Cdd:pfam17213  135 QSETPQISSSPPPAGPIQRRLSVSASVGGEEGLMSCVLPEDLLVEILAERIQLNDCHRGVVFDGL 199
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
1344-1491 3.20e-12

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: 73.23  E-value: 3.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQaLRERKKRELERLAREMHEKKLQQELERQ 1423
Cdd:pfam17380  389 QKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR-LEEERAREMERVRLEEQERQQQVERLRQ 467
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958748278 1424 KEEDELKRKVKRPKPGPVAKEEPPLKK----SQGPTNKQlpSVAKLEMKMESIERKVSVREHGLLEETTRKK 1491
Cdd:pfam17380  468 QEEERKRKKLELEKEKRDRKRAEEQRRkileKELEERKQ--AMIEEERKRKLLEKEMEERQKAIYEEERRRE 537
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1343-1511 5.06e-09

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: 61.47  E-value: 5.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1343 MKAQEKAKKELEETKRQEALAKEKERLQTLDEE----EYDALTAEQKIAFDREvRQALRERKKRELERLAR--------- 1409
Cdd:pfam13868  122 LEKQRQLREEIDEFNEEQAEWKELEKEEEREEDerilEYLKEKAEREEEREAE-REEIEEEKEREIARLRAqqekaqdek 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1410 ----EMHEKKLQQELE---RQKEEDELKRKVKRpkpgpvaKEEppLKKSQgptNKQLpsvaKLEMKMESIERKvsvREHG 1482
Cdd:pfam13868  201 aerdELRAKLYQEEQErkeRQKEREEAEKKARQ-------RQE--LQQAR---EEQI----ELKERRLAEEAE---REEE 261
                          170       180
                   ....*....|....*....|....*....
gi 1958748278 1483 LLEETTRKKKatteyafgFPITQEQEESE 1511
Cdd:pfam13868  262 EFERMLRKQA--------EDEEIEQEEAE 282
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
1347-1435 2.48e-08

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: 54.92  E-value: 2.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1347 EKAKKELEE-TKRQEALAKEKERLQtldeEEYDALTAEQKIAfdREVRQALRERK---KRELERLAREMHEK-----KLQ 1417
Cdd:pfam20492   23 KKAQEELEEsEETAEELEEERRQAE----EEAERLEQKRQEA--EEEKERLEESAemeAEEKEQLEAELAEAqeeiaRLE 96
                           90
                   ....*....|....*....
gi 1958748278 1418 QELERQKEE-DELKRKVKR 1435
Cdd:pfam20492   97 EEVERKEEEaRRLQEELEE 115
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
1336-1611 2.58e-08

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: 60.14  E-value: 2.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1336 MSQDYVAMKAQEKAK-----KELEETK--------RQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQ---ALRER 1399
Cdd:pfam17380  296 MEQERLRQEKEEKAReverrRKLEEAEkarqaemdRQAAIYAEQERMAMERERELERIRQEERKRELERIRQeeiAMEIS 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1400 KKRELERLAREMHEK--KLQQELERQKE----EDELKRKVKRPKpgpvaKEEPPLKKSQgpTNKQLPSVAKLE------- 1466
Cdd:pfam17380  376 RMRELERLQMERQQKneRVRQELEAARKvkilEEERQRKIQQQK-----VEMEQIRAEQ--EEARQREVRRLEeerarem 448
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1467 --MKMESIERKVSVREHGLLEETTRKKKATTEYAfgfpiTQEQEESEgdflkdsdknlAQKFKVYDTCLKDVQNILMYWD 1544
Cdd:pfam17380  449 erVRLEEQERQQQVERLRQQEEERKRKKLELEKE-----KRDRKRAE-----------EQRRKILEKELEERKQAMIEEE 512
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958748278 1545 RKQGMMVPHTGPDEIP-HEVDDQRQAPSGGGGRKGRKDRERERLEKERAEKERLEREKAERERlEKLR 1611
Cdd:pfam17380  513 RKRKLLEKEMEERQKAiYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERER-EMMR 579
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1338-1527 3.43e-08

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: 58.78  E-value: 3.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1338 QDYVAMKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKK-L 1416
Cdd:pfam13868  158 LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQeL 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1417 QQELERQKEEDELKRKVKRpkpgpvAKEE----PPLKKSQGPTNKQLPSVAKLEMKMEsiERKVSVREhgLLEETTRKKK 1492
Cdd:pfam13868  238 QQAREEQIELKERRLAEEA------EREEeefeRMLRKQAEDEEIEQEEAEKRRMKRL--EHRRELEK--QIEEREEQRA 307
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1958748278 1493 AtteyafgfpiTQEQEESEGDFLKDSDKNLAQKFK 1527
Cdd:pfam13868  308 A----------EREEELEEGERLREEEAERRERIE 332
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
1347-1430 3.62e-08

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 55.43  E-value: 3.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1347 EKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAE---QKIAFDR-----EVRQALRERKKRELERLA--------RE 1410
Cdd:pfam05672   10 EEAARILAEKRRQAREQREREEQERLEKEEEERLRKEelrRRAEEERarreeEARRLEEERRREEEERQRkaeeeaeeRE 89
                           90       100
                   ....*....|....*....|
gi 1958748278 1411 MHEKKLQQELERQKEEDELK 1430
Cdd:pfam05672   90 QREQEEQERLQKQKEEAEAK 109
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1346-1435 9.59e-08

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: 57.24  E-value: 9.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1346 QEKAKKELEETKRQEALAK--EKERLQTLD-EEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQE-LE 1421
Cdd:pfam13868   29 AEKKRIKAEEKEEERRLDEmmEEERERALEeEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEiVE 108
                           90
                   ....*....|....
gi 1958748278 1422 RQKEEDELKRKVKR 1435
Cdd:pfam13868  109 RIQEEDQAEAEEKL 122
PTZ00121 PTZ00121
MAEBL; Provisional
1322-1491 1.00e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 1.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1322 LKAIGSREHIYVINMSQDYVAMKAqEKAKKELEETKRQEALAKEkerlqtldeEEYDALTAEQKIAFDREVRQAlRERKK 1401
Cdd:PTZ00121  1586 AKKAEEARIEEVMKLYEEEKKMKA-EEAKKAEEAKIKAEELKKA---------EEEKKKVEQLKKKEAEEKKKA-EELKK 1654
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1402 RELERLAREMHEKKLQQELERQKEEDELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLE-MKMESIERKVSVRE 1480
Cdd:PTZ00121  1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEeLKKAEEENKIKAEE 1734
                          170
                   ....*....|.
gi 1958748278 1481 HGLLEETTRKK 1491
Cdd:PTZ00121  1735 AKKEAEEDKKK 1745
PTZ00121 PTZ00121
MAEBL; Provisional
1337-1496 1.71e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 1.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1337 SQDYVAMKAQEKAKKELEETKRQEALAKEKE----RLQTLDEEEYDALTAEQ-KIAFDREVRQALRERKKRE-----LER 1406
Cdd:PTZ00121  1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEdekkAAEALKKEAEEAKKAEElKKKEAEEKKKAEELKKAEEenkikAEE 1734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1407 LAREMHEKKLQQElERQKEEDElKRKVKRPKPGPVAKEEPPLKKSQgptnkqlpSVAKLEMKMESIERKVSVrehgllEE 1486
Cdd:PTZ00121  1735 AKKEAEEDKKKAE-EAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKE--------AVIEEELDEEDEKRRMEV------DK 1798
                          170
                   ....*....|
gi 1958748278 1487 TTRKKKATTE 1496
Cdd:PTZ00121  1799 KIKDIFDNFA 1808
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
1344-1527 2.84e-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: 56.01  E-value: 2.84e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKKELEETKRQ--EALAKEKERLQTLDE---EEYDALTAEQ--KIAFDREvRQALRERKKRELERLARE--MHEK 1414
Cdd:TIGR02794   64 KKEQERQKKLEQQAEEaeKQRAAEQARQKELEQraaAEKAAKQAEQaaKQAEEKQ-KQAEEAKAKQAAEAKAKAeaEAER 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1415 KLQQELERQKEED-------ELKRKV----KRPKPGPVAKEEpPLKKSQGPTNKQLPSVAKLEMKMESIERKvsVREHGL 1483
Cdd:TIGR02794  143 KAKEEAAKQAEEEakakaaaEAKKKAeeakKKAEAEAKAKAE-AEAKAKAEEAKAKAEAAKAKAAAEAAAKA--EAEAAA 219
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1484 LEETTRKKKATTEYAFGFP------ITQEQEESEGDFLKDSDKNLAQKFK 1527
Cdd:TIGR02794  220 AAAAEAERKADEAELGDIFglasgsNAEKQGGARGAAAGSEVDKYAAIIQ 269
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
1345-1435 3.13e-07

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: 52.74  E-value: 3.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1345 AQEKAKKELEETKRQEALAKEKERLQTLDEEEydaltAEQKIAFDREvRQALRERKKRELERLAREMHEKKlQQELER-- 1422
Cdd:pfam05672   53 EEERARREEEARRLEEERRREEEERQRKAEEE-----AEEREQREQE-EQERLQKQKEEAEAKAREEAERQ-RQEREKim 125
                           90
                   ....*....|....
gi 1958748278 1423 QKEEDE-LKRKvKR 1435
Cdd:pfam05672  126 QQEEQErLERK-KR 138
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
1338-1491 3.21e-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: 55.62  E-value: 3.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1338 QDYVAMKAQEKAKKELEETKRQEALAKEKErlqtldEEEydaltAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQ 1417
Cdd:TIGR02794   99 AAEKAAKQAEQAAKQAEEKQKQAEEAKAKQ------AAE-----AKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKK 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1418 QELERQKEEDELK------RKVKRPKPGpvAKEEPPLKKSQGPTNKQLPSVAKLEMKMESiERKVSVRE----HGLLEET 1487
Cdd:TIGR02794  168 AEEAKKKAEAEAKakaeaeAKAKAEEAK--AKAEAAKAKAAAEAAAKAEAEAAAAAAAEA-ERKADEAElgdiFGLASGS 244

                   ....
gi 1958748278 1488 TRKK 1491
Cdd:TIGR02794  245 NAEK 248
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1345-1493 3.29e-07

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 56.20  E-value: 3.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1345 AQEKAKKELEETKRQEALAKEKERLQTLDEEEYDAL--TAEQKIAFDREVRQALRE--RKKRELERLAREMHEKKLQQEL 1420
Cdd:COG3064      1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKeeAEEERLAELEAKRQAEEEarEAKAEAEQRAAELAAEAAKKLA 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958748278 1421 ERQKEEDELKRKVKRPKPGPVAKEEPPLKKsqgptnKQLPSVAKLEmKMESIERKVsvrehglleETTRKKKA 1493
Cdd:COG3064     81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAA------EKAAAAAEKE-KAEEAKRKA---------EEEAKRKA 137
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
1346-1510 4.61e-07

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: 56.11  E-value: 4.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1346 QEKAKK-----ELEETKRQEALAKEKERLQtlDEEEYDaltaEQKIAFDREVRQALRERKKR---ELERLAREMHEKKLQ 1417
Cdd:pfam15709  368 LERAEKmreelELEQQRRFEEIRLRKQRLE--EERQRQ----EEEERKQRLQLQAAQERARQqqeEFRRKLQELQRKKQQ 441
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1418 QELERQKEEdelKRKVKrpkpgpvaKEEPPLKKSQgptnKQLPSVAKlEMKMESIERKVSVREHGLLE--ETTRKKKATT 1495
Cdd:pfam15709  442 EEAERAEAE---KQRQK--------ELEMQLAEEQ----KRLMEMAE-EERLEYQRQKQEAEEKARLEaeERRQKEEEAA 505
                          170
                   ....*....|....*
gi 1958748278 1496 EYAFGFPITQEQEES 1510
Cdd:pfam15709  506 RLALEEAMKQAQEQA 520
PTZ00121 PTZ00121
MAEBL; Provisional
1342-1493 1.15e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 1.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1342 AMKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRE-RKKRELERLAREMHEKKLQQEL 1420
Cdd:PTZ00121  1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKaEEAKKAEEAKKKAEEAKKADEA 1475
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958748278 1421 ERQKEE----DELKRKVKRPKpgpvAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKA 1493
Cdd:PTZ00121  1476 KKKAEEakkaDEAKKKAEEAK----KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
Caldesmon pfam02029
Caldesmon;
1337-1476 1.18e-06

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 54.49  E-value: 1.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1337 SQDYVAMK-AQEKAKKELEETKRqealaKEKERLQTLDEEEydaltaeqkiafdrevrqalRERKKRELERLAREMHEK- 1414
Cdd:pfam02029  262 SEEFEKLRqKQQEAELELEELKK-----KREERRKLLEEEE--------------------QRRKQEEAERKLREEEEKr 316
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958748278 1415 KLQQELERQKEEDELKRKvKRPKPGPvAKEEPPLKksqgPTNKQLPSVaKLEMKMESIERKV 1476
Cdd:pfam02029  317 RMKEEIERRRAEAAEKRQ-KLPEDSS-SEGKKPFK----CFSPKGSSL-KITERAEFLNKSL 371
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
1331-1445 1.33e-06

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 50.66  E-value: 1.33e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278  1331 IYVINMSQDYVAMKAQEKAKKELEET--KRQEALAKEKERLQTLdEEEYDA----LTAEQkiafdREVRQALRERKKREL 1404
Cdd:smart00935    1 IGVVDVQKILQESPAGKAAQKQLEKEfkKRQAELEKLEKELQKL-KEKLQKdaatLSEAA-----REKKEKELQKKVQEF 74
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1958748278  1405 ERLAREMHEK--KLQQElERQKEEDELKRKVKRpkpgpVAKEE 1445
Cdd:smart00935   75 QRKQQKLQQDlqKRQQE-ELQKILDKINKAIKE-----VAKKK 111
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
1359-1506 1.34e-06

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


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 51.23  E-value: 1.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1359 QEALAKEKERLQTLDEEEYDALTAEQkiafDREVRQALRERKKRELERLAREMHEKKlqqelERQKEEDELKRKVKRPKP 1438
Cdd:pfam11600    8 QSQEEKEKQRLEKDKERLRRQLKLEA----EKEEKERLKEEAKAEKERAKEEARRKK-----EEEKELKEKERREKKEKD 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1439 GPVAKEEPPLKKSQgPTNKQLPSVAKLEMKMESIERKvsvrehGLLEETTRKK--KATTEYAFGFPITQE 1506
Cdd:pfam11600   79 EKEKAEKLRLKEEK-RKEKQEALEAKLEEKRKKEEEK------RLKEEEKRIKaeKAEITRFLQKPKTQQ 141
PTZ00121 PTZ00121
MAEBL; Provisional
1342-1493 1.57e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 1.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1342 AMKAQEKAKKELEETKRQE------ALAKEKERLQTLDEEEYDALTAEQKIAFDrEVRQALRERK---------KRELER 1406
Cdd:PTZ00121  1228 AVKKAEEAKKDAEEAKKAEeernneEIRKFEEARMAHFARRQAAIKAEEARKAD-ELKKAEEKKKadeakkaeeKKKADE 1306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1407 LAREMHEKKLQQELERQKEE-----DELKRKV-KRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKL---EMKMESIERKVS 1477
Cdd:PTZ00121  1307 AKKKAEEAKKADEAKKKAEEakkkaDAAKKKAeEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKkkeEAKKKADAAKKK 1386
                          170
                   ....*....|....*.
gi 1958748278 1478 VREHGLLEETtrKKKA 1493
Cdd:PTZ00121  1387 AEEKKKADEA--KKKA 1400
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
1343-1426 1.71e-06

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: 49.92  E-value: 1.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1343 MKAQEKAKKELEEtKRQEALAkEKERLqtldeEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELER 1422
Cdd:pfam20492   43 RRQAEEEAERLEQ-KRQEAEE-EKERL-----EESAEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEE 115

                   ....
gi 1958748278 1423 QKEE 1426
Cdd:pfam20492  116 AREE 119
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
1366-1431 1.89e-06

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: 50.42  E-value: 1.89e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958748278 1366 KERLQTLDEEEYDALTAEQKiafdrevRQAlRERKKRE-LERLAREMHEKKLQQELERQKEEDELKR 1431
Cdd:pfam05672    1 KPSAGTTDAEEAARILAEKR-------RQA-REQREREeQERLEKEEEERLRKEELRRRAEEERARR 59
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
1342-1435 2.51e-06

Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar proteins; mS26, also known as mitochondrial 37S ribosomal protein PET12, is a component of the mitochondrial small ribosomal subunit (mt-SSU) of Saccharomyces cerevisiae mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. The family also includes a group of uncharacterized proteins from pezizomycotina, which show high sequence similarity with mS26.


Pssm-ID: 467916 [Multi-domain]  Cd Length: 179  Bit Score: 50.63  E-value: 2.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1342 AMKAQEKAKKELEETKRQ---EALAKEKERLQTLDEEEydaltaEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQ 1418
Cdd:cd23703     44 PLSEYQEWKRKMAELRRQnlrEGLRELEERKLKTEELR------AKRSERKQAERERALNAPEREDERLTLPTIESALLG 117
                           90       100
                   ....*....|....*....|..
gi 1958748278 1419 ELERQ-----KEEDELKRKVKR 1435
Cdd:cd23703    118 PLMRVrtdpeREERAAKRRANR 139
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
1341-1443 2.56e-06

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


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 50.46  E-value: 2.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1341 VAMKAQEKAKKELEETKRQealaKEKERLQTLDEEEYDaltAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQEL 1420
Cdd:pfam11600   48 EKERAKEEARRKKEEEKEL----KEKERREKKEKDEKE---KAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEE 120
                           90       100
                   ....*....|....*....|....
gi 1958748278 1421 ERQK-EEDELKRKVKRPKPGPVAK 1443
Cdd:pfam11600  121 KRIKaEKAEITRFLQKPKTQQAPK 144
Caldesmon pfam02029
Caldesmon;
1351-1434 3.58e-06

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 52.95  E-value: 3.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1351 KELEETKRQEA---LAKEKERLQTLDEEEYDALTAEQkiafdREVRQALRE-RKKRELERLAREMHE-KKLQQELERQKE 1425
Cdd:pfam02029  236 REEEAEVFLEAeqkLEELRRRRQEKESEEFEKLRQKQ-----QEAELELEElKKKREERRKLLEEEEqRRKQEEAERKLR 310

                   ....*....
gi 1958748278 1426 EDELKRKVK 1434
Cdd:pfam02029  311 EEEEKRRMK 319
PTZ00121 PTZ00121
MAEBL; Provisional
1344-1493 3.85e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 3.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKKElEETKRQEALAKEKERLQTLDEEEYDALTAEQKIafdREVRQALRERKKRELERLAREM----HEKKLQQE 1419
Cdd:PTZ00121  1386 KAEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKKADEAKKKA---EEKKKADEAKKKAEEAKKADEAkkkaEEAKKAEE 1461
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1420 LERQKEE----DELKRKVKRPKPGPVAKeepplKKSQGPTNK--QLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKA 1493
Cdd:PTZ00121  1462 AKKKAEEakkaDEAKKKAEEAKKADEAK-----KKAEEAKKKadEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
PTZ00121 PTZ00121
MAEBL; Provisional
1343-1493 4.02e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 4.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1343 MKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRE-RKKRELERLAREMHEKKLQQELE 1421
Cdd:PTZ00121  1410 LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKaEEAKKADEAKKKAEEAKKADEAK 1489
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958748278 1422 RQKEE-----DELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKA 1493
Cdd:PTZ00121  1490 KKAEEakkkaDEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1343-1435 4.70e-06

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: 51.84  E-value: 4.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1343 MKAQEKAKKELEETKRQEALAKEK--ERLQTLDEEEYdALTAEQKIAFDREVRQALRERKK-RELERLAREMHEKKLQQE 1419
Cdd:pfam13868   82 IEEREQKRQEEYEEKLQEREQMDEivERIQEEDQAEA-EEKLEKQRQLREEIDEFNEEQAEwKELEKEEEREEDERILEY 160
                           90
                   ....*....|....*.
gi 1958748278 1420 LeRQKEEDELKRKVKR 1435
Cdd:pfam13868  161 L-KEKAEREEEREAER 175
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1341-1525 4.80e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 4.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1341 VAMKAQEKAKKELEETKrqEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQEL 1420
Cdd:COG1196    257 ELEAELAELEAELEELR--LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1421 ERQKEEDELKRKvkrpkpgpvAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKATTEyafg 1500
Cdd:COG1196    335 LEEELEELEEEL---------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ---- 401
                          170       180
                   ....*....|....*....|....*
gi 1958748278 1501 fpiTQEQEESEGDFLKDSDKNLAQK 1525
Cdd:COG1196    402 ---LEELEEAEEALLERLERLEEEL 423
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1343-1540 5.37e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 53.05  E-value: 5.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1343 MKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEqkIAFDREVRQALRERKKRELERLAREMHE-KKLQQELE 1421
Cdd:pfam02463  254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE--EEELKSELLKLERRKVDDEEKLKESEKEkKKAEKELK 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1422 RQKEEDELKRKVKRPKPGPVAKEEppLKKSQgptnkqlpsvaklemkMESIERKVSVREHGLLEETTRKKKATTEYAfgf 1501
Cdd:pfam02463  332 KEKEEIEELEKELKELEIKREAEE--EEEEE----------------LEKLQEKLEQLEEELLAKKKLESERLSSAA--- 390
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1958748278 1502 pITQEQEESEGDFLKDSDKNLAQKFKVYDTCLKDVQNIL 1540
Cdd:pfam02463  391 -KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE 428
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
1317-1496 5.90e-06

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: 51.77  E-value: 5.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1317 ALICLLkAIGSREHIYVINMSQDYVAMKA----QEKAKKELEETKRQEALAKEKERlQTLDEEEYDALTAEQKIAFDREV 1392
Cdd:TIGR02794   13 LLLGLL-ILGSLYHSVKPEPGGGAEIIQAvlvdPGAVAQQANRIQQQKKPAAKKEQ-ERQKKLEQQAEEAEKQRAAEQAR 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1393 RQALRERKKRELErlAREMhEKKLQQELERQKEEDELKRKvkrPKPGPVAKEEPPL-KKSQGPTNKQLPSVAKLEMKMES 1471
Cdd:TIGR02794   91 QKELEQRAAAEKA--AKQA-EQAAKQAEEKQKQAEEAKAK---QAAEAKAKAEAEAeRKAKEEAAKQAEEEAKAKAAAEA 164
                          170       180
                   ....*....|....*....|....*
gi 1958748278 1472 ierKVSVREHGLLEETTRKKKATTE 1496
Cdd:TIGR02794  165 ---KKKAEEAKKKAEAEAKAKAEAE 186
PTZ00121 PTZ00121
MAEBL; Provisional
1344-1491 6.42e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 6.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKKELEETK-RQEALAK----EKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKlqQ 1418
Cdd:PTZ00121  1647 KKAEELKKAEEENKiKAAEEAKkaeeDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--A 1724
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958748278 1419 ELERQKEEDELKRKVKRPKpgpvaKEEPPLKKSQGPTNKQLPSVAKLEMKMESIER-KVSVREHGLLEETTRKK 1491
Cdd:PTZ00121  1725 EEENKIKAEEAKKEAEEDK-----KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKeKEAVIEEELDEEDEKRR 1793
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
1330-1493 9.23e-06

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 51.68  E-value: 9.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1330 HIYVINMSQDYVAMKAQEKAKKEleetkrqEALAKEKERLQTLDEEEYDALtaEQKIAFDREvrqALRERKKRELERLAR 1409
Cdd:pfam09731  293 HREIDQLSKKLAELKKREEKHIE-------RALEKQKEELDKLAEELSARL--EEVRAADEA---QLRLEFEREREEIRE 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1410 EMhEKKLQQELERQKE-------------EDELKRKVKRPKPGPVAKEEpplkksqgptNKQLPSVAKLEMKMESIERKV 1476
Cdd:pfam09731  361 SY-EEKLRTELERQAEaheehlkdvlveqEIELQREFLQDIKEKVEEER----------AGRLLKLNELLANLKGLEKAT 429
                          170
                   ....*....|....*..
gi 1958748278 1477 SvrEHGLLEETTRKKKA 1493
Cdd:pfam09731  430 S--SHSEVEDENRKAQQ 444
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
1328-1438 9.86e-06

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 47.56  E-value: 9.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1328 REhIYVINMSQDyvaMKAQEKAKKELEETKRQEALAKEKERLQTlDEEEYDALTAEQkiafDREVRQALRERKKRELERL 1407
Cdd:pfam13863    6 RE-MFLVQLALD---AKREEIERLEELLKQREEELEKKEQELKE-DLIKFDKFLKEN----DAKRRRALKKAEEETKLKK 76
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958748278 1408 AREMHEKKLQQELER-QKEEDELKRKVKRPKP 1438
Cdd:pfam13863   77 EKEKEIKKLTAQIEElKSEISKLEEKLEEYKP 108
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
1338-1432 1.09e-05

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


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 48.12  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1338 QDYVAMKAQEKAKKELEET--KRQEALAKEkerLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELErlaremhEKK 1415
Cdd:pfam15346    9 EEETARRVEEAVAKRVEEEleKRKDEIEAE---VERRVEEARKIMEKQVLEELEREREAELEEERRKEEE-------ERK 78
                           90       100
                   ....*....|....*....|..
gi 1958748278 1416 LQQELER-----QKEEDELKRK 1432
Cdd:pfam15346   79 KREELERileenNRKIEEAQRK 100
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
1331-1445 1.71e-05

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 47.57  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1331 IYVINMSQDYVAMKAQEKAKKELEE--TKRQEALAKEKERLQTLdeeeYDALTAEQKIAfdrevrQALRERKKRELERLA 1408
Cdd:pfam03938    2 IGYVDMQKILEESPEGKAAQAQLEKkfKKRQAELEAKQKELQKL----YEELQKDGALL------EEEREEKEQELQKKE 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1958748278 1409 REMHE--KKLQQELERQKEE------DELKRKVKRpkpgpVAKEE 1445
Cdd:pfam03938   72 QELQQlqQKAQQELQKKQQEllqpiqDKINKAIKE-----VAKEK 111
Caldesmon pfam02029
Caldesmon;
1349-1515 2.00e-05

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 50.64  E-value: 2.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1349 AKKELEETKR-QEALAKEKERLQTL-DEEEYDALTAE--QKIAFDREVRQALRER-----KKRELERLAREMHEKKLQQE 1419
Cdd:pfam02029   69 AKREERRQKRlQEALERQKEFDPTIaDEKESVAERKEnnEEEENSSWEKEEKRDSrlgryKEEETEIREKEYQENKWSTE 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1420 LERQKE---EDELKRKVKRPKPGPV-AKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREhgllEETTRKKKATT 1495
Cdd:pfam02029  149 VRQAEEegeEEEDKSEEAEEVPTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGE----EEVTKLKVTTK 224
                          170       180
                   ....*....|....*....|
gi 1958748278 1496 EYAFGFPITQEQEESEGDFL 1515
Cdd:pfam02029  225 RRQGGLSQSQEREEEAEVFL 244
PRK12704 PRK12704
phosphodiesterase; Provisional
1344-1475 2.00e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 50.55  E-value: 2.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKKELEETKRQ-EALAKEKErLQTldEEEYDALTAEqkiaFDREVRQalrerKKRELERLaremhEKKLQQELER 1422
Cdd:PRK12704    35 EAEEEAKRILEEAKKEaEAIKKEAL-LEA--KEEIHKLRNE----FEKELRE-----RRNELQKL-----EKRLLQKEEN 97
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958748278 1423 QKEEDELkrkvkrpkpgpVAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERK 1475
Cdd:PRK12704    98 LDRKLEL-----------LEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
1342-1434 3.06e-05

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 49.21  E-value: 3.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1342 AMKAQEKAKKEleETKRQEALAKEKERLQTLDEEEyDALTAEQKIAFDREVRQaLRERKKRELERLAREmHEKKLQQELE 1421
Cdd:pfam02841  198 ALTAKEKAIEA--ERAKAEAAEAEQELLREKQKEE-EQMMEAQERSYQEHVKQ-LIEKMEAEREQLLAE-QERMLEHKLQ 272
                           90
                   ....*....|....*
gi 1958748278 1422 RQKE--EDELKRKVK 1434
Cdd:pfam02841  273 EQEEllKEGFKTEAE 287
PTZ00121 PTZ00121
MAEBL; Provisional
1325-1493 3.53e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 3.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1325 IGSREHIYVINMSQDYVAMKAQEKAK----KELEETKRQEALAKEKERlQTLDEEEYdalTAEQKIAFDREVRQAlrERK 1400
Cdd:PTZ00121  1254 IRKFEEARMAHFARRQAAIKAEEARKadelKKAEEKKKADEAKKAEEK-KKADEAKK---KAEEAKKADEAKKKA--EEA 1327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1401 KRELERLAREMHEKKLQQELERQKEE---DELKRKVKRPKPGPVAKEEPplKKSQGPTNKQLPSVAKL-EMKMESIERKV 1476
Cdd:PTZ00121  1328 KKKADAAKKKAEEAKKAAEAAKAEAEaaaDEAEAAEEKAEAAEKKKEEA--KKKADAAKKKAEEKKKAdEAKKKAEEDKK 1405
                          170
                   ....*....|....*..
gi 1958748278 1477 SVREhgLLEETTRKKKA 1493
Cdd:PTZ00121  1406 KADE--LKKAAAAKKKA 1420
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1342-1431 3.83e-05

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: 49.15  E-value: 3.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1342 AMKAQEKAKKElEETKRQEALAK---EKERLQTLDEEEYDaLTAEQKIAFDREVR---QALRERKKRELERLAREM---- 1411
Cdd:pfam13868   59 EEEEKEEERKE-ERKRYRQELEEqieEREQKRQEEYEEKL-QEREQMDEIVERIQeedQAEAEEKLEKQRQLREEIdefn 136
                           90       100
                   ....*....|....*....|
gi 1958748278 1412 HEKKLQQELERQKEEDELKR 1431
Cdd:pfam13868  137 EEQAEWKELEKEEEREEDER 156
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
1347-1432 5.17e-05

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


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 48.88  E-value: 5.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1347 EKAKKELEETKR-QEALAKEKER-LQTLDEEEYDAL-----TAEQKiafdREVRqALRERKKRELERLAREMHEKKLQQE 1419
Cdd:pfam15558  112 ERARQEAEQRKQcQEQRLKEKEEeLQALREQNSLQLqerleEACHK----RQLK-EREEQKKVQENNLSELLNHQARKVL 186
                           90
                   ....*....|....
gi 1958748278 1420 LERQ-KEEDELKRK 1432
Cdd:pfam15558  187 VDCQaKAEELLRRL 200
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
1344-1437 5.62e-05

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 48.34  E-value: 5.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQaLRERKKRELERLARE---MHEKKLQQEL 1420
Cdd:cd16269    191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQ-LKEKMEEERENLLKEqerALESKLKEQE 269
                           90       100
                   ....*....|....*....|..
gi 1958748278 1421 ERQKEE-----DELKRKVKRPK 1437
Cdd:cd16269    270 ALLEEGfkeqaELLQEEIRSLK 291
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1344-1495 5.93e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 48.88  E-value: 5.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKK-ELEETKRQEALAKEKERLQTldEEEYDALTAEQKIAfDREVRQALRERKKRELERLAREMHEKKLQQelER 1422
Cdd:COG3064     52 QAEEEAREaKAEAEQRAAELAAEAAKKLA--EAEKAAAEAEKKAA-AEKAKAAKEAEAAAAAEKAAAAAEKEKAEE--AK 126
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958748278 1423 QKEEDELKRKVKRPKPGpVAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKATT 1495
Cdd:COG3064    127 RKAEEEAKRKAEEERKA-AEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAA 198
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1342-1435 6.54e-05

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: 48.38  E-value: 6.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1342 AMKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERK-------KRELERLAREMHEK 1414
Cdd:pfam13868  226 EAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRrmkrlehRRELEKQIEEREEQ 305
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1958748278 1415 KL----------QQELERQKEEDELKRKVKR 1435
Cdd:pfam13868  306 RAaereeeleegERLREEEAERRERIEEERQ 336
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1341-1435 6.95e-05

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: 48.38  E-value: 6.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1341 VAMKAQEKAKKELEETKRQEALAKEKERL-----------QTLDE--EEYDALTAEQKIAFDREvRQALRERKKRELE-- 1405
Cdd:pfam13868   36 AEEKEEERRLDEMMEEERERALEEEEEKEeerkeerkryrQELEEqiEEREQKRQEEYEEKLQE-REQMDEIVERIQEed 114
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958748278 1406 -RLAREMHEKK--LQQELERQKEEDELKRKVKR 1435
Cdd:pfam13868  115 qAEAEEKLEKQrqLREEIDEFNEEQAEWKELEK 147
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1342-1446 7.87e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 48.50  E-value: 7.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1342 AMKAQEKAKKELEETKRQEAlakEKERLQTLD-----EEEYDALTAEQKIAFDRevRQALRERKKRELERLAREMhEKKL 1416
Cdd:COG3064     20 QAEAEKRAAAEAEQKAKEEA---EEERLAELEakrqaEEEAREAKAEAEQRAAE--LAAEAAKKLAEAEKAAAEA-EKKA 93
                           90       100       110
                   ....*....|....*....|....*....|
gi 1958748278 1417 QQELERQKEEDElkRKVKRPKPGPVAKEEP 1446
Cdd:COG3064     94 AAEKAKAAKEAE--AAAAAEKAAAAAEKEK 121
Cgr1 pfam03879
Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA ...
1337-1437 8.25e-05

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


Pssm-ID: 427562 [Multi-domain]  Cd Length: 107  Bit Score: 44.54  E-value: 8.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1337 SQDYVAMKAQEKAKKELEETKRQEALAKEKErLQTLDEEEydaltAEQKIAFDREvRQALRERKKReLERLAREMHEKKL 1416
Cdd:pfam03879   21 SSLVVGPKSKSWEKRQEKRLELKAIKAKEKE-LKDEKEAE-----RQRRIQAIKE-RREAKEEKER-YEELAAKMHAKKV 92
                           90       100
                   ....*....|....*....|.
gi 1958748278 1417 QQelerqkeedeLKRKVKRPK 1437
Cdd:pfam03879   93 ER----------LKRKEKRNK 103
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
1344-1454 9.02e-05

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 48.86  E-value: 9.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKKELEETKRQ--------------EALAKEKERLQTLDEEEYDALTAEQKIafdrEVRQALRERKKRELERLAR 1409
Cdd:NF033838   315 EAKKKAKDQKEEDRRNyptntyktleleiaESDVKVKEAELELVKEEAKEPRNEEKI----KQAKAKVESKKAEATRLEK 390
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958748278 1410 EMHEKKLQQELERQK--EEDELKRK-VKRPKPGPVAKEEPPLKKSQGP 1454
Cdd:NF033838   391 IKTDRKKAEEEAKRKaaEEDKVKEKpAEQPQPAPAPQPEKPAPKPEKP 438
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1328-1435 1.12e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1328 REHIYVINMSQDYVAMKAQEKAKKELEETkrQEALAKEKERLQTLdEEEYDALTAEQkiafdREVRQALRERKKRELERL 1407
Cdd:COG4913    272 AELEYLRAALRLWFAQRRLELLEAELEEL--RAELARLEAELERL-EARLDALREEL-----DELEAQIRGNGGDRLEQL 343
                           90       100
                   ....*....|....*....|....*...
gi 1958748278 1408 AREMHEKKLQQElERQKEEDELKRKVKR 1435
Cdd:COG4913    344 EREIERLERELE-ERERRRARLEALLAA 370
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1344-1531 1.12e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 48.43  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDaltaEQKIAFDREVRQALRERKKRELERLAREmhEKKLQQELERQ 1423
Cdd:pfam02463  201 KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLN----EERIDLLQELLRDEQEEIESSKQEIEKE--EEKLAQVLKEN 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1424 KEEdELKRKVKRPKPGPVAKEEppLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKAtTEYAFGFPI 1503
Cdd:pfam02463  275 KEE-EKEKKLQEEELKLLAKEE--EELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELE-KELKELEIK 350
                          170       180
                   ....*....|....*....|....*...
gi 1958748278 1504 TQEQEESEGDFLKDSDKNLAQKFKVYDT 1531
Cdd:pfam02463  351 REAEEEEEEELEKLQEKLEQLEEELLAK 378
YscO pfam07321
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ...
1340-1429 1.16e-04

Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.


Pssm-ID: 399954 [Multi-domain]  Cd Length: 148  Bit Score: 45.08  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1340 YVAMKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDAlTAEQKIAFDREVRQALRERkKRELERLAreMHEKKLQQE 1419
Cdd:pfam07321   55 YAEIQGKLVLLKELEKVKQQVALLRENEADLEKQVAEARQ-QLEAEREALRQARQALAEA-RRAVEKFA--ELVRLVQAE 130
                           90
                   ....*....|...
gi 1958748278 1420 LERQ---KEEDEL 1429
Cdd:pfam07321  131 ELRQqerQEEQEL 143
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
1347-1434 1.30e-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: 47.61  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1347 EKAKKELEETKRQEALAKEKERLQtlDEEEYDALtaEQKIAFDREVRQALRERKKRELERLAREmhekklqQELERQKEE 1426
Cdd:pfam13868  264 ERMLRKQAEDEEIEQEEAEKRRMK--RLEHRREL--EKQIEEREEQRAAEREEELEEGERLREE-------EAERRERIE 332

                   ....*...
gi 1958748278 1427 DELKRKVK 1434
Cdd:pfam13868  333 EERQKKLK 340
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
1344-1432 1.39e-04

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


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 47.34  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEydaltaeqkiafdrEVRQALRERKKREL-ERLAREMHeKKLQQELER 1422
Cdd:pfam15558  101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKE--------------EELQALREQNSLQLqERLEEACH-KRQLKEREE 165
                           90
                   ....*....|
gi 1958748278 1423 QKEEDELKRK 1432
Cdd:pfam15558  166 QKKVQENNLS 175
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
1338-1493 1.45e-04

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


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 47.34  E-value: 1.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1338 QDYVAMKAQEKAKKELEetKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAR-----EMH 1412
Cdd:pfam15558   26 LQQQAALAWEELRRRDQ--KRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRwreqaEDQ 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1413 EKKLQQELERQKEEDELKRK--VKRPKpgpvAKEEppLKKSQGPTNKQLpsvakLEMKMESIERKVSVREHGL---LEET 1487
Cdd:pfam15558  104 ENQRQEKLERARQEAEQRKQcqEQRLK----EKEE--ELQALREQNSLQ-----LQERLEEACHKRQLKEREEqkkVQEN 172

                   ....*.
gi 1958748278 1488 TRKKKA 1493
Cdd:pfam15558  173 NLSELL 178
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1342-1530 1.80e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 1.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1342 AMKAQEKAKKELEETKRQ-----EALAKEKERLQTLdEEEYDALTAE-QKIAFDREVRQALRERKKRELERLAREMHEKK 1415
Cdd:COG4372     71 ARSELEQLEEELEELNEQlqaaqAELAQAQEELESL-QEEAEELQEElEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1416 LQ-QELERQKE--EDELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEET-TRKK 1491
Cdd:COG4372    150 EElKELEEQLEslQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKdSLEA 229
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1958748278 1492 KATTEYAFGFPITQEQEESEGDFLKDSDKNLAQKFKVYD 1530
Cdd:COG4372    230 KLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
1338-1569 2.03e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 47.66  E-value: 2.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1338 QDYVAMKAQEKAKKELEETKRQEAlakekerlqtldEEEYDALTaeQKIAFDREVRQALRERK----------KRELERL 1407
Cdd:TIGR00618  424 GQLAHAKKQQELQQRYAELCAAAI------------TCTAQCEK--LEKIHLQESAQSLKEREqqlqtkeqihLQETRKK 489
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1408 AREMHEKKLQQELERqkeedELKRKVKRPKPGPVAKEEPPLkkSQGPTNKQLPSVAKLEMKMESIerkvsvrEHGLLEET 1487
Cdd:TIGR00618  490 AVVLARLLELQEEPC-----PLCGSCIHPNPARQDIDNPGP--LTRRMQRGEQTYAQLETSEEDV-------YHQLTSER 555
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1488 TRKKkatteyafgfpITQEQEESEgdflKDSDKNLAQKFKVYDTCLKDVQNI---LMYW------DRKQGMMVPHTGPDE 1558
Cdd:TIGR00618  556 KQRA-----------SLKEQMQEI----QQSFSILTQCDNRSKEDIPNLQNItvrLQDLteklseAEDMLACEQHALLRK 620
                          250
                   ....*....|.
gi 1958748278 1559 IPHEVDDQRQA 1569
Cdd:TIGR00618  621 LQPEQDLQDVR 631
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
1342-1496 2.33e-04

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 46.96  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1342 AMKAQEKAKKELEETKRQEALAKEKERLQtldeeeydaltAEQKIAFDREVRQAlRERKKRELERLAremhEKKLQQELE 1421
Cdd:COG3064     75 AAKKLAEAEKAAAEAEKKAAAEKAKAAKE-----------AEAAAAAEKAAAAA-EKEKAEEAKRKA----EEEAKRKAE 138
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958748278 1422 RQKEEDELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKATTE 1496
Cdd:COG3064    139 EERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
1346-1523 2.57e-04

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: 47.48  E-value: 2.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1346 QEKAKKELEE-TKRQEALAKEKERLQtldeeeyDALTAEQKIAFDREVRQALRERKKRELERLAREMhEKKLQQELERQK 1424
Cdd:pfam01576   21 QQKAESELKElEKKHQQLCEEKNALQ-------EQLQAETELCAEAEEMRARLAARKQELEEILHEL-ESRLEEEEERSQ 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1425 EEDELKRKVKRpkpgPVAKEEPPLKKSQGPTNK-QLPSVAkLEMKMESIERKVSV---------REHGLLEEttRKKKAT 1494
Cdd:pfam01576   93 QLQNEKKKMQQ----HIQDLEEQLDEEEAARQKlQLEKVT-TEAKIKKLEEDILLledqnsklsKERKLLEE--RISEFT 165
                          170       180
                   ....*....|....*....|....*....
gi 1958748278 1495 TEYAfgfpitqEQEESEGDFLKDSDKNLA 1523
Cdd:pfam01576  166 SNLA-------EEEEKAKSLSKLKNKHEA 187
Saf4_Yju2 pfam04502
Saf4/Yju2 protein; This is a family of eukaryotic proteins that includes CCDC130 and CCDC94 ...
1342-1525 2.74e-04

Saf4/Yju2 protein; This is a family of eukaryotic proteins that includes CCDC130 and CCDC94 from humans, Saf4 from fission yeasts and Yju2 from budding yeasts. Saf4 (also known as cwc16) is involved in mRNA splicing where it associates with cdc5 and the other cwf proteins as part of the spliceosome. Yju2 is a splicing factor that is associated with the Prp 19-associated complex and acts after Prp2 in promoting the first catalytic reaction of pre-mRNA splicing.


Pssm-ID: 461333 [Multi-domain]  Cd Length: 328  Bit Score: 46.20  E-value: 2.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1342 AMKAQEK----AKKELEETKRQEALAKEKERLQTLDeeeYDALtaeqkiafdREVRQALR-ERKKRELERLAREMHEKKL 1416
Cdd:pfam04502  130 AMKKLEKrtkdSKREMEALERLEELQELNQRQWKDD---YDAN---------LKLRREFReEKKEREEEEEDEEALKEKM 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1417 QQE-LERQKEEDELKRKVK------------RPKPGPVAKEEPPLKKSQGPTNKqlpsVAKLEMKMESIERKVSVREHGL 1483
Cdd:pfam04502  198 SLEiIKLLPEDEEDDRRAAlvefgsrplfgdSSPPAKTESPTDSLTSEISASSK----RESLKKSLGKLTRKAADPLLLG 273
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958748278 1484 LeetTRKKKATTEYAFGFPITQEQEESEGDFLKDSDKNLAQK 1525
Cdd:pfam04502  274 V---KRKKAATEEPSTPSSETSTESSKTSTPSSAQVSSSSPA 312
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1347-1493 3.22e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 3.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1347 EKAKKELEETKRQeaLAKEKERLQTLdEEEYDALTAEQKiafdrEVRQALrERKKRELERLAREMheKKLQQELER-QKE 1425
Cdd:COG4372     62 EQLEEELEQARSE--LEQLEEELEEL-NEQLQAAQAELA-----QAQEEL-ESLQEEAEELQEEL--EELQKERQDlEQQ 130
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958748278 1426 EDELKRKVKRPKPGPVAKEEpplkksqgptnkQLpsvAKLEMKMESIERKVSVREHGLLEETTRKKKA 1493
Cdd:COG4372    131 RKQLEAQIAELQSEIAEREE------------EL---KELEEQLESLQEELAALEQELQALSEAEAEQ 183
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1347-1435 3.50e-04

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: 45.30  E-value: 3.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1347 EKAKKELEETKRQEALAKEKERLQTL-DEEEYDALTAEqkIAFDREVRQALRERKKRELERLarEMHEKKLQQ-ELERQK 1424
Cdd:COG1579     60 EIKRLELEIEEVEARIKKYEEQLGNVrNNKEYEALQKE--IESLKRRISDLEDEILELMERI--EELEEELAElEAELAE 135
                           90
                   ....*....|.
gi 1958748278 1425 EEDELKRKVKR 1435
Cdd:COG1579    136 LEAELEEKKAE 146
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
1300-1454 6.03e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.59  E-value: 6.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1300 GVVFDGLDTLFARNAPSALIcllkaigSRehIYVIN--MSQDYVAMKAQEKAKKELEETKrqEALAKEKERLQTL-DEEE 1376
Cdd:COG3883     99 GGSVSYLDVLLGSESFSDFL-------DR--LSALSkiADADADLLEELKADKAELEAKK--AELEAKLAELEALkAELE 167
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958748278 1377 YDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELERQKEEDELKRKVKRPKPGPVAKEEPPLKKSQGP 1454
Cdd:COG3883    168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
1342-1427 6.04e-04

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: 43.25  E-value: 6.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1342 AMKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDA--LTAEQKiAFDREVRQALR-----ERKKREL-------ERL 1407
Cdd:pfam15236   54 ALEHQNAIKKQLEEKERQKKLEEERRRQEEQEEEERLRreREEEQK-QFEEERRKQKEkeeamTRKTQALlqamqkaQEL 132
                           90       100
                   ....*....|....*....|
gi 1958748278 1408 AREMHEKKLQQELErQKEED 1427
Cdd:pfam15236  133 AQRLKQEQRIRELA-EKGHD 151
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
1347-1435 6.45e-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: 42.21  E-value: 6.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1347 EKAKKELEE---------TKRQEALAKEKERLQTLDEEEYDAltaeqkiafdREVRQALrERKKRELERLAREMHEKKLQ 1417
Cdd:pfam20492    5 EREKQELEErlkqyeeetKKAQEELEESEETAEELEEERRQA----------EEEAERL-EQKRQEAEEEKERLEESAEM 73
                           90       100
                   ....*....|....*....|.
gi 1958748278 1418 QELERQKEEDEL---KRKVKR 1435
Cdd:pfam20492   74 EAEEKEQLEAELaeaQEEIAR 94
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
1280-1336 6.65e-04

Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440329 [Multi-domain]  Cd Length: 212  Bit Score: 43.96  E-value: 6.65e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1280 PDDLLIQILAERIQLSDCFRGVVFDGldtlFARNAPSALIclLKAIGSREHI---YVINM 1336
Cdd:COG0563     60 PDEIVIGLVKERLAQPDCANGFILDG----FPRTVAQAEA--LDELLAELGIkldAVIEL 113
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
1343-1452 6.78e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.97  E-value: 6.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1343 MKAQEKAK---KELEETKR-QEALAKEKERLQtldeEEYDALTAEQKiafdREVRQALRERKKrELERLAREMHEK-KLQ 1417
Cdd:PRK00409   530 RELEQKAEeaeALLKEAEKlKEELEEKKEKLQ----EEEDKLLEEAE----KEAQQAIKEAKK-EADEIIKELRQLqKGG 600
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958748278 1418 QELERQKEEDELKRKVKRPKPgpvAKEEPPLKKSQ 1452
Cdd:PRK00409   601 YASVKAHELIEARKRLNKANE---KKEKKKKKQKE 632
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
1338-1435 9.44e-04

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


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 45.03  E-value: 9.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1338 QDYVAMKAQEKAKKELEETKR-----------QEALAKEKERlQTLDEEEYDALTAEQKIAFDREVRQALRERKKREL-E 1405
Cdd:pfam15558  148 QERLEEACHKRQLKEREEQKKvqennlsellnHQARKVLVDC-QAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELrE 226
                           90       100       110
                   ....*....|....*....|....*....|
gi 1958748278 1406 RLAREmhEKKLQQELERQKEEDELKRKVKR 1435
Cdd:pfam15558  227 KAQKE--EEQFQRAKWRAEEKEEERQEHKE 254
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1373-1498 1.19e-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: 43.76  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1373 DEEEYDALTAEQKIafDREVRQALRERKK--RELERLAREMheKKLQQELERQKEE-DELKRKVKRpKPGPVAKEEPPLK 1449
Cdd:COG1579      2 MPEDLRALLDLQEL--DSELDRLEHRLKElpAELAELEDEL--AALEARLEAAKTElEDLEKEIKR-LELEIEEVEARIK 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958748278 1450 KSQgptnKQLPSVAK------LEMKMESIERKVSVREHGLLEETTRKKKATTEYA 1498
Cdd:COG1579     77 KYE----EQLGNVRNnkeyeaLQKEIESLKRRISDLEDEILELMERIEELEEELA 127
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1344-1435 1.20e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELERQ 1423
Cdd:COG1196    666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
                           90       100
                   ....*....|....*....|....*.
gi 1958748278 1424 KE--------------EDELKRKVKR 1435
Cdd:COG1196    746 ELleeealeelpeppdLEELERELER 771
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
1350-1613 1.26e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.11  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1350 KKELEETKRQEALAK-EKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKR---ELERLAREMhekklQQELERQKE 1425
Cdd:pfam17380  281 QKAVSERQQQEKFEKmEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyaEQERMAMER-----ERELERIRQ 355
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1426 EDElKRKVKRPKPGPVAKEeppLKKSQGPTNKQLPSVAKLEMKMESIErkvSVREHGLLEETtRKKKATTEYAFGFPITQ 1505
Cdd:pfam17380  356 EER-KRELERIRQEEIAME---ISRMRELERLQMERQQKNERVRQELE---AARKVKILEEE-RQRKIQQQKVEMEQIRA 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1506 EQEESEGDFLKDSDKNLAQKfkvydtclkdvqnilMYWDRKQGMmvphtgpdEIPHEVDDQRQAPSGGGGRKGRKDRERe 1585
Cdd:pfam17380  428 EQEEARQREVRRLEEERARE---------------MERVRLEEQ--------ERQQQVERLRQQEEERKRKKLELEKEK- 483
                          250       260
                   ....*....|....*....|....*...
gi 1958748278 1586 rleKERAEKERLEREKAERERLEKLRAM 1613
Cdd:pfam17380  484 ---RDRKRAEEQRRKILEKELEERKQAM 508
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
1343-1434 1.44e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.41  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1343 MKAQEKAK-KELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELE 1421
Cdd:PRK09510   103 LKQLEKERlAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE 182
                           90
                   ....*....|....
gi 1958748278 1422 RQKE-EDELKRKVK 1434
Cdd:PRK09510   183 AKKKaEAEAAAKAA 196
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1341-1435 1.58e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1341 VAMKAQEKaKKELEETKRQEALAKEKERLQTLD--EEEYDALTAE-QKIAFDREVRQALRERKKRELERLAREMHEKKlQ 1417
Cdd:COG1196    211 KAERYREL-KEELKELEAELLLLKLRELEAELEelEAELEELEAElEELEAELAELEAELEELRLELEELELELEEAQ-A 288
                           90
                   ....*....|....*...
gi 1958748278 1418 QELERQKEEDELKRKVKR 1435
Cdd:COG1196    289 EEYELLAELARLEQDIAR 306
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
1348-1450 1.70e-03

Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and tropomyosin binding (TnT). this Pfam contains members of the TnT subunit. Troponin is a complex of three proteins, Ca2+ binding (TnC), inhibitory (TnI), and tropomyosin binding (TnT). The troponin complex regulates Ca++ induced muscle contraction. This family includes troponin T and troponin I. Troponin I binds to actin and troponin T binds to tropomyosin.


Pssm-ID: 460018 [Multi-domain]  Cd Length: 132  Bit Score: 41.40  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1348 KAKKELEetkrQEALAKEKERLQTLDEEeydaltaEQKIAFDREVRQALRERKKRELERLAREMHEK--KLQQELERQKE 1425
Cdd:pfam00992   11 KAAEELE----FEQEKKEEEKLRYLAER-------IPPLRLRGLSAEQLQELCEELHERIDKLEEERydIEEKVAKKDKE 79
                           90       100
                   ....*....|....*....|....*..
gi 1958748278 1426 EDELKRKV--KRPKPGPvakeePPLKK 1450
Cdd:pfam00992   80 INDLKKKVndLRGKFKK-----PLLKK 101
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
1346-1440 1.79e-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: 43.15  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1346 QEKAKKELEETKRQEaLAKE--------KERLQTLDEEEYDALTAEQKIAFDR----------EVRQAL----------- 1396
Cdd:pfam13904   77 EEREKEEQEAELRKR-LAKEkyqewlqrKARQQTKKREESHKQKAAESASKSLakperkvsqeEAKEVLqewerkkleqq 155
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958748278 1397 ---RERKKRElerlaremhEKKLQQELERQKEEDELK-----RKVK-RPKPGP 1440
Cdd:pfam13904  156 qrkREEEQRE---------QLKKEEEEQERKQLAEKAwqkwmKNVKnKPKPVP 199
adk PRK00279
adenylate kinase; Reviewed
1280-1336 1.82e-03

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 42.83  E-value: 1.82e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958748278 1280 PDDLLIQILAERIQLSDCFRGVVFDGldtlFARNAP--SALICLLKAIGsREHIYVINM 1336
Cdd:PRK00279    60 PDEIVIGLVKERLAQPDCKNGFLLDG----FPRTIPqaEALDEMLKELG-IKLDAVIEI 113
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1346-1435 1.93e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1346 QEKAKKELEETKRQ-EALAKEKERLQTLDEEEYDALTAEQKiafDREVRQALRERKKRELERLAREM-HEKKLQQELERQ 1423
Cdd:COG1196    241 LEELEAELEELEAElEELEAELAELEAELEELRLELEELEL---ELEEAQAEEYELLAELARLEQDIaRLEERRRELEER 317
                           90
                   ....*....|..
gi 1958748278 1424 KEEDELKRKVKR 1435
Cdd:COG1196    318 LEELEEELAELE 329
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1342-1431 2.21e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 2.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1342 AMKAQEKAKKELEETKRQEALAKEKERLQTLDE-----EEYDALTAEQkiafdREVRQALrERKKRELERLAREMheKKL 1416
Cdd:COG4717    161 LEEELEELEAELAELQEELEELLEQLSLATEEElqdlaEELEELQQRL-----AELEEEL-EEAQEELEELEEEL--EQL 232
                           90
                   ....*....|....*
gi 1958748278 1417 QQELERQKEEDELKR 1431
Cdd:COG4717    233 ENELEAAALEERLKE 247
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1321-1525 3.31e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.81  E-value: 3.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1321 LLKAIG-SREHIYVINMSQDY--VAMKAQEKAKKELEETKRQEALAKEKERLQTLDEEeydALTAEQKIAFDREVRQALR 1397
Cdd:pfam02463  124 LLESQGiSPEAYNFLVQGGKIeiIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEE---TENLAELIIDLEELKLQEL 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1398 ERKKRELERLAREMHEKKLQQELERQKEEDELKRKVKRpkpgpvakeeppLKKSQGPTNKQLPSVAKLEMKMESIERKvS 1477
Cdd:pfam02463  201 KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER------------IDLLQELLRDEQEEIESSKQEIEKEEEK-L 267
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958748278 1478 VREHGLLEETTRKKKATTEYAfGFPITQEQEESEGDFLKDSDKNLAQK 1525
Cdd:pfam02463  268 AQVLKENKEEEKEKKLQEEEL-KLLAKEEEELKSELLKLERRKVDDEE 314
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
1344-1429 3.38e-03

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 442129 [Multi-domain]  Cd Length: 142  Bit Score: 40.66  E-value: 3.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKKELeeTKRQEALAKEKERLQTLDE--EEY---------------------------DALTAEQKIAFDR---- 1390
Cdd:COG2882     16 KEEDEAAREL--GQAQQALEQAEEQLEQLEQyrEEYeqrlqqklqqglsaaqlrnyqqfiarlDEAIEQQQQQVAQaeqq 93
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1958748278 1391 --EVRQALRERKKRE--LERLaREMHEKKLQQELER--QKEEDEL 1429
Cdd:COG2882     94 veQARQAWLEARQERkaLEKL-KERRREEERQEENRreQKELDEL 137
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1342-1426 3.63e-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: 42.83  E-value: 3.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1342 AMKAQEKAKKELEETKRQeaLAKEKERLQTLDEEEYDAL----TAEQKIAFDREVRQALRER---KKRELERLAREmhEK 1414
Cdd:COG4942     18 QADAAAEAEAELEQLQQE--IAELEKELAALKKEEKALLkqlaALERRIAALARRIRALEQElaaLEAELAELEKE--IA 93
                           90
                   ....*....|..
gi 1958748278 1415 KLQQELERQKEE 1426
Cdd:COG4942     94 ELRAELEAQKEE 105
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1344-1435 4.26e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 4.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKKELEE-TKRQEALakekERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKrELERLAREmhEKKLQQELER 1422
Cdd:COG4913    631 ERLEALEAELDAlQERREAL----QRLAEYSWDEIDVASAEREIAELEAELERLDASSD-DLAALEEQ--LEELEAELEE 703
                           90
                   ....*....|....
gi 1958748278 1423 QKEE-DELKRKVKR 1435
Cdd:COG4913    704 LEEElDELKGEIGR 717
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1347-1491 5.85e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 5.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1347 EKAKKELEE-TKRQEALAKEKERLQTLDEEEYDALTAEQKI----AFDREVRQALRER------KKRELERLAREmhEKK 1415
Cdd:PRK03918   272 KKEIEELEEkVKELKELKEKAEEYIKLSEFYEEYLDELREIekrlSRLEEEINGIEERikeleeKEERLEELKKK--LKE 349
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958748278 1416 LQQELERQKEEDELKRKVKRPKpgpvaKEEPPLKKSQGPTNKQlpsvaKLEMKMESIE-RKVSVREHglLEETTRKK 1491
Cdd:PRK03918   350 LEKRLEELEERHELYEEAKAKK-----EELERLKKRLTGLTPE-----KLEKELEELEkAKEEIEEE--ISKITARI 414
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1344-1432 6.02e-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: 6.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1344 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELERQ 1423
Cdd:COG1196    366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445

                   ....*....
gi 1958748278 1424 KEEDELKRK 1432
Cdd:COG1196    446 EAAEEEAEL 454
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1343-1453 7.74e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 7.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1343 MKAQEKAKKELEE-TKRQEALAKEKERLQTlDEEEYDalTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELE 1421
Cdd:PRK03918   330 IKELEEKEERLEElKKKLKELEKRLEELEE-RHELYE--EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEE 406
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958748278 1422 RQKEED---ELKRKVKRPKPgpvAKEEppLKKSQG 1453
Cdd:PRK03918   407 ISKITArigELKKEIKELKK---AIEE--LKKAKG 436
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
1347-1432 8.52e-03

B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains


Pssm-ID: 128778  Cd Length: 127  Bit Score: 39.17  E-value: 8.52e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278  1347 EKAKKELEETKRqeALAKEKERLQTLdEEEYDALTAEQKIAFDrEVRQALRERKKRELERL--AREMHEKKLQQELER-Q 1423
Cdd:smart00502   10 TKLRKKAAELED--ALKQLISIIQEV-EENAADVEAQIKAAFD-ELRNALNKRKKQLLEDLeeQKENKLKVLEQQLESlT 85

                    ....*....
gi 1958748278  1424 KEEDELKRK 1432
Cdd:smart00502   86 QKQEKLSHA 94
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
1383-1508 8.98e-03

CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.


Pssm-ID: 461894 [Multi-domain]  Cd Length: 202  Bit Score: 40.69  E-value: 8.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1383 EQKI-AFDREVRQALRERKKR---------ELERLAREMHEKKLQqeLERQKEEDELKRKVKrpkpgpvAKEE--PPLKK 1450
Cdd:pfam06391   67 EKKIeQYEKENKDLILKNKMKlsqeeeeleELLELEKREKEERRK--EEKQEEEEEKEKKEK-------AKQEliDELMT 137
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958748278 1451 SQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKATTEYAFGFPITQEQE 1508
Cdd:pfam06391  138 SNKDAEEIIAQHKKTAKKRKSERRRKLEELNRVLEQKPTQFSTGIKFGQLPVPKIEEG 195
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1321-1498 9.42e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 9.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1321 LLKAIGSREHIYVINMSQDYVAMKAQEKAKKELEE-TKRQEALAKEKERLQTLDEE---EYDALTAEQKIAFDREVRQAL 1396
Cdd:COG4717     58 LFKPQGRKPELNLKELKELEEELKEAEEKEEEYAElQEELEELEEELEELEAELEElreELEKLEKLLQLLPLYQELEAL 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1397 RERKKRELERLAREMHEKKLQQELERQKEE-----DELKRKVKRpkpgpvAKEEPPLKKSQgptnkqlpSVAKLEMKMES 1471
Cdd:COG4717    138 EAELAELPERLEELEERLEELRELEEELEEleaelAELQEELEE------LLEQLSLATEE--------ELQDLAEELEE 203
                          170       180
                   ....*....|....*....|....*..
gi 1958748278 1472 IERKVSVREHGLLEETTRKKKATTEYA 1498
Cdd:COG4717    204 LQQRLAELEEELEEAQEELEELEEELE 230
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
1342-1435 9.83e-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: 39.77  E-value: 9.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748278 1342 AMKAQEKAKKELEETKRQ---------EALAKEKERLQTLDEEEYDALT--AEQKIAfdREVRQALRErKKRELERLARE 1410
Cdd:COG0711     50 AEAALAEYEEKLAEARAEaaeiiaearKEAEAIAEEAKAEAEAEAERIIaqAEAEIE--QERAKALAE-LRAEVADLAVA 126
                           90       100
                   ....*....|....*....|....*
gi 1958748278 1411 MHEKKLQQELERQKEEDELKRKVKR 1435
Cdd:COG0711    127 IAEKILGKELDAAAQAALVDRFIAE 151
 
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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