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Conserved domains on  [gi|1958748272|ref|XP_038954163|]
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hydrocephalus-inducing protein homolog isoform X3 [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 ...
2005-2229 6.73e-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: 6.73e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2005 AIIVYGTPVSGKTANAISMAKFYNTACLNIDSIVLEALSDSNNVLGIRARELCIRAAIEQSMREAEESAQESSVTQNLGA 2084
Cdd:pfam17213    1 AIIVHGAPLSGKTATAVTLAKHYGAACLTIDSIVLEAISDGNSIAGLRARELCARAAIEQSEREAEEAAQEAAVVPGQPT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2085 PARLSTENLGRFTSDLTLLTQEYKIPKSMRGSVMLSKGKTESHWSGSqkqqgqqqqqqqqqqpqqqqqpqqqqQQQHHQH 2164
Cdd:pfam17213   81 TYRLSVEALTKHTSEGTLVGPESKISKGKRGSVVSGKGKADSHGTGS--------------------------QKQHHQH 134
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958748272 2165 QSETPQISSSPLLGGPTQRRLSVSASIGGETGLMSCVLPDDLLIQILAERIQLSDCFRGVVFDGL 2229
Cdd:pfam17213  135 QSETPQISSSPPPAGPIQRRLSVSASVGGEEGLMSCVLPEDLLVEILAERIQLNDCHRGVVFDGL 199
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
538-637 3.10e-17

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.


:

Pssm-ID: 464865 [Multi-domain]  Cd Length: 98  Bit Score: 80.02  E-value: 3.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272  538 EGIIEPSGVQAvQIAFSSTSLGHFEEEFLIDVNGSPEPVkLTIRGCVIGPTFHFNVPALHFgNVSYGFPHTLTCSLNNTS 617
Cdd:pfam15780    2 VLLLAPFSRQP-FVCFGDVPVGTSAERLLTVVNPSEEPA-EVKVSKVPAPTKGFSVSPLEF-TVQPGESQTLTVTWTPTE 78
                           90       100
                   ....*....|....*....|
gi 1958748272  618 LVSMTFKLRVRGDGEGMSSI 637
Cdd:pfam15780   79 EGAVRETLQFTVNDVGKHQV 98
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2267-2414 3.31e-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: 3.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2267 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQaLRERKKRELERLAREMHEKKLQQELERQ 2346
Cdd:pfam17380  389 QKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR-LEEERAREMERVRLEEQERQQQVERLRQ 467
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958748272 2347 KEEDELKRKVKRPKPGPVAKEEPPLKK----SQGPTNKQlpSVAKLEMKMESIERKVSVREHGLLEETTRKK 2414
Cdd:pfam17380  468 QEEERKRKKLELEKEKRDRKRAEEQRRkileKELEERKQ--AMIEEERKRKLLEKEMEERQKAIYEEERRRE 537
Motile_Sperm super family cl44412
MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These ...
227-302 3.67e-05

MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These proteins oligomerise to form filaments. This family contains many other proteins.


The actual alignment was detected with superfamily member pfam00635:

Pssm-ID: 459882  Cd Length: 109  Bit Score: 45.82  E-value: 3.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272  227 PDELNFSTCPVKYSTQKvLLVRNIGNKDSMFHLKTRSP--YSVEPTGGILNVGESMQLEVNFEPQTVG-----NHsgKLI 299
Cdd:pfam00635    7 PDLIFFAAPGNKQGTST-LTLKNTSDKRVAFKVKTTNPkkYRVRPNYGIIKPGESVTITITRQPFDEEpgdakKD--KFV 83

                   ...
gi 1958748272  300 VIY 302
Cdd:pfam00635   84 IQY 86
Adk super family cl33950
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
2203-2259 8.16e-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: 8.16e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2203 PDDLLIQILAERIQLSDCFRGVVFDGldtlFARNAPSALIclLKAIGSREHI---YVINM 2259
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 ...
2005-2229 6.73e-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: 6.73e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2005 AIIVYGTPVSGKTANAISMAKFYNTACLNIDSIVLEALSDSNNVLGIRARELCIRAAIEQSMREAEESAQESSVTQNLGA 2084
Cdd:pfam17213    1 AIIVHGAPLSGKTATAVTLAKHYGAACLTIDSIVLEAISDGNSIAGLRARELCARAAIEQSEREAEEAAQEAAVVPGQPT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2085 PARLSTENLGRFTSDLTLLTQEYKIPKSMRGSVMLSKGKTESHWSGSqkqqgqqqqqqqqqqpqqqqqpqqqqQQQHHQH 2164
Cdd:pfam17213   81 TYRLSVEALTKHTSEGTLVGPESKISKGKRGSVVSGKGKADSHGTGS--------------------------QKQHHQH 134
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958748272 2165 QSETPQISSSPLLGGPTQRRLSVSASIGGETGLMSCVLPDDLLIQILAERIQLSDCFRGVVFDGL 2229
Cdd:pfam17213  135 QSETPQISSSPPPAGPIQRRLSVSASVGGEEGLMSCVLPEDLLVEILAERIQLNDCHRGVVFDGL 199
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
538-637 3.10e-17

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.


Pssm-ID: 464865 [Multi-domain]  Cd Length: 98  Bit Score: 80.02  E-value: 3.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272  538 EGIIEPSGVQAvQIAFSSTSLGHFEEEFLIDVNGSPEPVkLTIRGCVIGPTFHFNVPALHFgNVSYGFPHTLTCSLNNTS 617
Cdd:pfam15780    2 VLLLAPFSRQP-FVCFGDVPVGTSAERLLTVVNPSEEPA-EVKVSKVPAPTKGFSVSPLEF-TVQPGESQTLTVTWTPTE 78
                           90       100
                   ....*....|....*....|
gi 1958748272  618 LVSMTFKLRVRGDGEGMSSI 637
Cdd:pfam15780   79 EGAVRETLQFTVNDVGKHQV 98
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2267-2414 3.31e-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: 3.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2267 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQaLRERKKRELERLAREMHEKKLQQELERQ 2346
Cdd:pfam17380  389 QKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR-LEEERAREMERVRLEEQERQQQVERLRQ 467
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958748272 2347 KEEDELKRKVKRPKPGPVAKEEPPLKK----SQGPTNKQlpSVAKLEMKMESIERKVSVREHGLLEETTRKK 2414
Cdd:pfam17380  468 QEEERKRKKLELEKEKRDRKRAEEQRRkileKELEERKQ--AMIEEERKRKLLEKEMEERQKAIYEEERRRE 537
PTZ00121 PTZ00121
MAEBL; Provisional
2245-2414 9.44e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 9.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2245 LKAIGSREHIYVINMSQDYVAMKAqEKAKKELEETKRQEALAKEkerlqtldeEEYDALTAEQKIAFDREVRQAlRERKK 2324
Cdd:PTZ00121  1586 AKKAEEARIEEVMKLYEEEKKMKA-EEAKKAEEAKIKAEELKKA---------EEEKKKVEQLKKKEAEEKKKA-EELKK 1654
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2325 RELERLAREMHEKKLQQELERQKEEDELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLE-MKMESIERKVSVRE 2403
Cdd:PTZ00121  1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEeLKKAEEENKIKAEE 1734
                          170
                   ....*....|.
gi 1958748272 2404 HGLLEETTRKK 2414
Cdd:PTZ00121  1735 AKKEAEEDKKK 1745
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
2267-2450 3.49e-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: 3.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2267 KAQEKAKKELEETKRQ--EALAKEKERLQTLDE---EEYDALTAEQ--KIAFDREvRQALRERKKRELERLARE--MHEK 2337
Cdd:TIGR02794   64 KKEQERQKKLEQQAEEaeKQRAAEQARQKELEQraaAEKAAKQAEQaaKQAEEKQ-KQAEEAKAKQAAEAKAKAeaEAER 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2338 KLQQELERQKEED-------ELKRKV----KRPKPGPVAKEEpPLKKSQGPTNKQLPSVAKLEMKMESIERKvsVREHGL 2406
Cdd:TIGR02794  143 KAKEEAAKQAEEEakakaaaEAKKKAeeakKKAEAEAKAKAE-AEAKAKAEEAKAKAEAAKAKAAAEAAAKA--EAEAAA 219
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2407 LEETTRKKKATTEYAFGFP------ITQEQEESEGDFLKDSDKNLAQKFK 2450
Cdd:TIGR02794  220 AAAAEAERKADEAELGDIFglasgsNAEKQGGARGAAAGSEVDKYAAIIQ 269
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
2268-2416 4.05e-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: 4.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2268 AQEKAKKELEETKRQEALAKEKERLQTLDEEEYDAL--TAEQKIAFDREVRQALRE--RKKRELERLAREMHEKKLQQEL 2343
Cdd:COG3064      1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKeeAEEERLAELEAKRQAEEEarEAKAEAEQRAAELAAEAAKKLA 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958748272 2344 ERQKEEDELKRKVKRPKPGPVAKEEPPLKKsqgptnKQLPSVAKLEmKMESIERKVsvrehglleETTRKKKA 2416
Cdd:COG3064     81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAA------EKAAAAAEKE-KAEEAKRKA---------EEEAKRKA 137
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
2254-2368 1.05e-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: 51.05  E-value: 1.05e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272  2254 IYVINMSQDYVAMKAQEKAKKELEET--KRQEALAKEKERLQTLdEEEYDA----LTAEQkiafdREVRQALRERKKREL 2327
Cdd:smart00935    1 IGVVDVQKILQESPAGKAAQKQLEKEfkKRQAELEKLEKELQKL-KEKLQKdaatLSEAA-----REKKEKELQKKVQEF 74
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1958748272  2328 ERLAREMHEK--KLQQElERQKEEDELKRKVKRpkpgpVAKEE 2368
Cdd:smart00935   75 QRKQQKLQQDlqKRQQE-ELQKILDKINKAIKE-----VAKKK 111
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
2265-2358 2.53e-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: 51.02  E-value: 2.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2265 AMKAQEKAKKELEETKRQ---EALAKEKERLQTLDEEEydaltaEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQ 2341
Cdd:cd23703     44 PLSEYQEWKRKMAELRRQnlrEGLRELEERKLKTEELR------AKRSERKQAERERALNAPEREDERLTLPTIESALLG 117
                           90       100
                   ....*....|....*....|..
gi 1958748272 2342 ELERQ-----KEEDELKRKVKR 2358
Cdd:cd23703    118 PLMRVrtdpeREERAAKRRANR 139
Motile_Sperm pfam00635
MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These ...
227-302 3.67e-05

MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These proteins oligomerise to form filaments. This family contains many other proteins.


Pssm-ID: 459882  Cd Length: 109  Bit Score: 45.82  E-value: 3.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272  227 PDELNFSTCPVKYSTQKvLLVRNIGNKDSMFHLKTRSP--YSVEPTGGILNVGESMQLEVNFEPQTVG-----NHsgKLI 299
Cdd:pfam00635    7 PDLIFFAAPGNKQGTST-LTLKNTSDKRVAFKVKTTNPkkYRVRPNYGIIKPGESVTITITRQPFDEEpgdakKD--KFV 83

                   ...
gi 1958748272  300 VIY 302
Cdd:pfam00635   84 IQY 86
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
2267-2377 1.11e-04

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: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2267 KAQEKAKKELEETKRQ--------------EALAKEKERLQTLDEEEYDALTAEQKIafdrEVRQALRERKKRELERLAR 2332
Cdd:NF033838   315 EAKKKAKDQKEEDRRNyptntyktleleiaESDVKVKEAELELVKEEAKEPRNEEKI----KQAKAKVESKKAEATRLEK 390
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958748272 2333 EMHEKKLQQELERQK--EEDELKRK-VKRPKPGPVAKEEPPLKKSQGP 2377
Cdd:NF033838   391 IKTDRKKAEEEAKRKaaEEDKVKEKpAEQPQPAPAPQPEKPAPKPEKP 438
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
2203-2259 8.16e-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: 8.16e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2203 PDDLLIQILAERIQLSDCFRGVVFDGldtlFARNAPSALIclLKAIGSREHI---YVINM 2259
Cdd:COG0563     60 PDEIVIGLVKERLAQPDCANGFILDG----FPRTVAQAEA--LDELLAELGIkldAVIEL 113
adk PRK00279
adenylate kinase; Reviewed
2203-2259 2.23e-03

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 42.83  E-value: 2.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958748272 2203 PDDLLIQILAERIQLSDCFRGVVFDGldtlFARNAP--SALICLLKAIGsREHIYVINM 2259
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 ...
2005-2229 6.73e-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: 6.73e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2005 AIIVYGTPVSGKTANAISMAKFYNTACLNIDSIVLEALSDSNNVLGIRARELCIRAAIEQSMREAEESAQESSVTQNLGA 2084
Cdd:pfam17213    1 AIIVHGAPLSGKTATAVTLAKHYGAACLTIDSIVLEAISDGNSIAGLRARELCARAAIEQSEREAEEAAQEAAVVPGQPT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2085 PARLSTENLGRFTSDLTLLTQEYKIPKSMRGSVMLSKGKTESHWSGSqkqqgqqqqqqqqqqpqqqqqpqqqqQQQHHQH 2164
Cdd:pfam17213   81 TYRLSVEALTKHTSEGTLVGPESKISKGKRGSVVSGKGKADSHGTGS--------------------------QKQHHQH 134
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958748272 2165 QSETPQISSSPLLGGPTQRRLSVSASIGGETGLMSCVLPDDLLIQILAERIQLSDCFRGVVFDGL 2229
Cdd:pfam17213  135 QSETPQISSSPPPAGPIQRRLSVSASVGGEEGLMSCVLPEDLLVEILAERIQLNDCHRGVVFDGL 199
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
538-637 3.10e-17

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.


Pssm-ID: 464865 [Multi-domain]  Cd Length: 98  Bit Score: 80.02  E-value: 3.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272  538 EGIIEPSGVQAvQIAFSSTSLGHFEEEFLIDVNGSPEPVkLTIRGCVIGPTFHFNVPALHFgNVSYGFPHTLTCSLNNTS 617
Cdd:pfam15780    2 VLLLAPFSRQP-FVCFGDVPVGTSAERLLTVVNPSEEPA-EVKVSKVPAPTKGFSVSPLEF-TVQPGESQTLTVTWTPTE 78
                           90       100
                   ....*....|....*....|
gi 1958748272  618 LVSMTFKLRVRGDGEGMSSI 637
Cdd:pfam15780   79 EGAVRETLQFTVNDVGKHQV 98
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2267-2414 3.31e-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: 3.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2267 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQaLRERKKRELERLAREMHEKKLQQELERQ 2346
Cdd:pfam17380  389 QKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR-LEEERAREMERVRLEEQERQQQVERLRQ 467
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958748272 2347 KEEDELKRKVKRPKPGPVAKEEPPLKK----SQGPTNKQlpSVAKLEMKMESIERKVSVREHGLLEETTRKK 2414
Cdd:pfam17380  468 QEEERKRKKLELEKEKRDRKRAEEQRRkileKELEERKQ--AMIEEERKRKLLEKEMEERQKAIYEEERRRE 537
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2266-2434 2.53e-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: 62.63  E-value: 2.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2266 MKAQEKAKKELEETKRQEALAKEKERLQTLDEE----EYDALTAEQKIAFDREvRQALRERKKRELERLAR--------- 2332
Cdd:pfam13868  122 LEKQRQLREEIDEFNEEQAEWKELEKEEEREEDerilEYLKEKAEREEEREAE-REEIEEEKEREIARLRAqqekaqdek 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2333 ----EMHEKKLQQELE---RQKEEDELKRKVKRpkpgpvaKEEppLKKSQgptNKQLpsvaKLEMKMESIERKvsvREHG 2405
Cdd:pfam13868  201 aerdELRAKLYQEEQErkeRQKEREEAEKKARQ-------RQE--LQQAR---EEQI----ELKERRLAEEAE---REEE 261
                          170       180
                   ....*....|....*....|....*....
gi 1958748272 2406 LLEETTRKKKatteyafgFPITQEQEESE 2434
Cdd:pfam13868  262 EFERMLRKQA--------EDEEIEQEEAE 282
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
2269-2363 1.12e-08

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: 58.95  E-value: 1.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2269 QEKAKKELEETKRQEaLAKE--------KERLQTLDEEEYDALTAEQKIAFDR----------EVRQALRE--RKKRELE 2328
Cdd:pfam13904   77 EEREKEEQEAELRKR-LAKEkyqewlqrKARQQTKKREESHKQKAAESASKSLakperkvsqeEAKEVLQEweRKKLEQQ 155
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1958748272 2329 ---RLAREMHEKKLQQELERQKEEDELK-----RKVK-RPKPGP 2363
Cdd:pfam13904  156 qrkREEEQREQLKKEEEEQERKQLAEKAwqkwmKNVKnKPKPVP 199
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
2270-2358 1.48e-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: 56.08  E-value: 1.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2270 EKAKKELEE-TKRQEALAKEKERLQtldeEEYDALTAEQKIAfdREVRQALRERK---KRELERLAREMHEK-----KLQ 2340
Cdd:pfam20492   23 KKAQEELEEsEETAEELEEERRQAE----EEAERLEQKRQEA--EEEKERLEESAemeAEEKEQLEAELAEAqeeiaRLE 96
                           90
                   ....*....|....*....
gi 1958748272 2341 QELERQKEE-DELKRKVKR 2358
Cdd:pfam20492   97 EEVERKEEEaRRLQEELEE 115
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2261-2450 1.90e-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: 59.93  E-value: 1.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2261 QDYVAMKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKK-L 2339
Cdd:pfam13868  158 LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQeL 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2340 QQELERQKEEDELKRKVKRpkpgpvAKEE----PPLKKSQGPTNKQLPSVAKLEMKMEsiERKVSVREhgLLEETTRKKK 2415
Cdd:pfam13868  238 QQAREEQIELKERRLAEEA------EREEeefeRMLRKQAEDEEIEQEEAEKRRMKRL--EHRRELEK--QIEEREEQRA 307
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1958748272 2416 AtteyafgfpiTQEQEESEGDFLKDSDKNLAQKFK 2450
Cdd:pfam13868  308 A----------EREEELEEGERLREEEAERRERIE 332
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
2270-2353 2.69e-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: 56.20  E-value: 2.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2270 EKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAE---QKIAFDR-----EVRQALRERKKRELERLA--------RE 2333
Cdd:pfam05672   10 EEAARILAEKRRQAREQREREEQERLEKEEEERLRKEelrRRAEEERarreeEARRLEEERRREEEERQRkaeeeaeeRE 89
                           90       100
                   ....*....|....*....|
gi 1958748272 2334 MHEKKLQQELERQKEEDELK 2353
Cdd:pfam05672   90 QREQEEQERLQKQKEEAEAK 109
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2259-2534 2.71e-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: 60.52  E-value: 2.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2259 MSQDYVAMKAQEKAK-----KELEETK--------RQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQ---ALRER 2322
Cdd:pfam17380  296 MEQERLRQEKEEKAReverrRKLEEAEkarqaemdRQAAIYAEQERMAMERERELERIRQEERKRELERIRQeeiAMEIS 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2323 KKRELERLAREMHEK--KLQQELE---RQK-EEDELKRKVKRPKpgpvaKEEPPLKKSQgpTNKQLPSVAKLE------- 2389
Cdd:pfam17380  376 RMRELERLQMERQQKneRVRQELEaarKVKiLEEERQRKIQQQK-----VEMEQIRAEQ--EEARQREVRRLEeerarem 448
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2390 --MKMESIERKVSVREHGLLEETTRKKKATTEYAfgfpiTQEQEESEgdflkdsdknlAQKFKVYDTCLKDVQNILMYWD 2467
Cdd:pfam17380  449 erVRLEEQERQQQVERLRQQEEERKRKKLELEKE-----KRDRKRAE-----------EQRRKILEKELEERKQAMIEEE 512
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958748272 2468 RKQGMMVPHTGPDEIP-HEVDDQRQAPSGGGGRKGRKDRERERLEKERAEKERLEREKAERERlEKLR 2534
Cdd:pfam17380  513 RKRKLLEKEMEERQKAiYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERER-EMMR 579
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2269-2358 6.94e-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: 58.01  E-value: 6.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2269 QEKAKKELEETKRQEALAK--EKERLQTLD-EEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQE-LE 2344
Cdd:pfam13868   29 AEKKRIKAEEKEEERRLDEmmEEERERALEeEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEiVE 108
                           90
                   ....*....|....
gi 1958748272 2345 RQKEEDELKRKVKR 2358
Cdd:pfam13868  109 RIQEEDQAEAEEKL 122
PTZ00121 PTZ00121
MAEBL; Provisional
2245-2414 9.44e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 9.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2245 LKAIGSREHIYVINMSQDYVAMKAqEKAKKELEETKRQEALAKEkerlqtldeEEYDALTAEQKIAFDREVRQAlRERKK 2324
Cdd:PTZ00121  1586 AKKAEEARIEEVMKLYEEEKKMKA-EEAKKAEEAKIKAEELKKA---------EEEKKKVEQLKKKEAEEKKKA-EELKK 1654
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2325 RELERLAREMHEKKLQQELERQKEEDELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLE-MKMESIERKVSVRE 2403
Cdd:PTZ00121  1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEeLKKAEEENKIKAEE 1734
                          170
                   ....*....|.
gi 1958748272 2404 HGLLEETTRKK 2414
Cdd:PTZ00121  1735 AKKEAEEDKKK 1745
PTZ00121 PTZ00121
MAEBL; Provisional
2260-2419 1.50e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 1.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2260 SQDYVAMKAQEKAKKELEETKRQEALAKEKE----RLQTLDEEEYDALTAEQ-KIAFDREVRQALRERKKRE-----LER 2329
Cdd:PTZ00121  1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEdekkAAEALKKEAEEAKKAEElKKKEAEEKKKAEELKKAEEenkikAEE 1734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2330 LAREMHEKKLQQElERQKEEDElKRKVKRPKPGPVAKEEPPLKKSQgptnkqlpSVAKLEMKMESIERKVSVrehgllEE 2409
Cdd:PTZ00121  1735 AKKEAEEDKKKAE-EAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKE--------AVIEEELDEEDEKRRMEV------DK 1798
                          170
                   ....*....|
gi 1958748272 2410 TTRKKKATTE 2419
Cdd:PTZ00121  1799 KIKDIFDNFA 1808
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
2268-2358 2.24e-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: 53.51  E-value: 2.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2268 AQEKAKKELEETKRQEALAKEKERLQTLDEEEydaltAEQKIAFDREvRQALRERKKRELERLAREMHEKKlQQELER-- 2345
Cdd:pfam05672   53 EEERARREEEARRLEEERRREEEERQRKAEEE-----AEEREQREQE-EQERLQKQKEEAEAKAREEAERQ-RQEREKim 125
                           90
                   ....*....|....
gi 1958748272 2346 QKEEDE-LKRKvKR 2358
Cdd:pfam05672  126 QQEEQErLERK-KR 138
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
2269-2433 3.43e-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: 56.50  E-value: 3.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2269 QEKAKK-----ELEETKRQEALAKEKERLQtlDEEEYDaltaEQKIAFDREVRQALRERKKR---ELERLAREMHEKKLQ 2340
Cdd:pfam15709  368 LERAEKmreelELEQQRRFEEIRLRKQRLE--EERQRQ----EEEERKQRLQLQAAQERARQqqeEFRRKLQELQRKKQQ 441
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2341 QELERQKEEdelKRKVKrpkpgpvaKEEPPLKKSQgptnKQLPSVAKlEMKMESIERKVSVREHGLLE--ETTRKKKATT 2418
Cdd:pfam15709  442 EEAERAEAE---KQRQK--------ELEMQLAEEQ----KRLMEMAE-EERLEYQRQKQEAEEKARLEaeERRQKEEEAA 505
                          170
                   ....*....|....*
gi 1958748272 2419 EYAFGFPITQEQEES 2433
Cdd:pfam15709  506 RLALEEAMKQAQEQA 520
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
2267-2450 3.49e-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: 3.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2267 KAQEKAKKELEETKRQ--EALAKEKERLQTLDE---EEYDALTAEQ--KIAFDREvRQALRERKKRELERLARE--MHEK 2337
Cdd:TIGR02794   64 KKEQERQKKLEQQAEEaeKQRAAEQARQKELEQraaAEKAAKQAEQaaKQAEEKQ-KQAEEAKAKQAAEAKAKAeaEAER 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2338 KLQQELERQKEED-------ELKRKV----KRPKPGPVAKEEpPLKKSQGPTNKQLPSVAKLEMKMESIERKvsVREHGL 2406
Cdd:TIGR02794  143 KAKEEAAKQAEEEakakaaaEAKKKAeeakKKAEAEAKAKAE-AEAKAKAEEAKAKAEAAKAKAAAEAAAKA--EAEAAA 219
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2407 LEETTRKKKATTEYAFGFP------ITQEQEESEGDFLKDSDKNLAQKFK 2450
Cdd:TIGR02794  220 AAAAEAERKADEAELGDIFglasgsNAEKQGGARGAAAGSEVDKYAAIIQ 269
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
2261-2414 3.95e-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: 3.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2261 QDYVAMKAQEKAKKELEETKRQEALAKEKErlqtldEEEydaltAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQ 2340
Cdd:TIGR02794   99 AAEKAAKQAEQAAKQAEEKQKQAEEAKAKQ------AAE-----AKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKK 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2341 QELERQKEEDELK------RKVKRPKPGpvAKEEPPLKKSQGPTNKQLPSVAKLEMKMESiERKVSVRE----HGLLEET 2410
Cdd:TIGR02794  168 AEEAKKKAEAEAKakaeaeAKAKAEEAK--AKAEAAKAKAAAEAAAKAEAEAAAAAAAEA-ERKADEAElgdiFGLASGS 244

                   ....
gi 1958748272 2411 TRKK 2414
Cdd:TIGR02794  245 NAEK 248
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
2268-2416 4.05e-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: 4.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2268 AQEKAKKELEETKRQEALAKEKERLQTLDEEEYDAL--TAEQKIAFDREVRQALRE--RKKRELERLAREMHEKKLQQEL 2343
Cdd:COG3064      1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKeeAEEERLAELEAKRQAEEEarEAKAEAEQRAAELAAEAAKKLA 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958748272 2344 ERQKEEDELKRKVKRPKPGPVAKEEPPLKKsqgptnKQLPSVAKLEmKMESIERKVsvrehglleETTRKKKA 2416
Cdd:COG3064     81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAA------EKAAAAAEKE-KAEEAKRKA---------EEEAKRKA 137
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
2282-2429 6.65e-07

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: 52.38  E-value: 6.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2282 QEALAKEKERLQTLDEEEYDALTAEQkiafDREVRQALRERKKRELERLAREMHEKKlqqelERQKEEDELKRKVKRPKP 2361
Cdd:pfam11600    8 QSQEEKEKQRLEKDKERLRRQLKLEA----EKEEKERLKEEAKAEKERAKEEARRKK-----EEEKELKEKERREKKEKD 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2362 GPVAKEEPPLKKSQgPTNKQLPSVAKLEMKMESIERKvsvrehGLLEETTRKK--KATTEYAFGFPITQE 2429
Cdd:pfam11600   79 EKEKAEKLRLKEEK-RKEKQEALEAKLEEKRKKEEEK------RLKEEEKRIKaeKAEITRFLQKPKTQQ 141
Caldesmon pfam02029
Caldesmon;
2260-2399 9.10e-07

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 55.26  E-value: 9.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2260 SQDYVAMK-AQEKAKKELEETKRqealaKEKERLQTLDEEEydaltaeqkiafdrevrqalRERKKRELERLAREMHEK- 2337
Cdd:pfam02029  262 SEEFEKLRqKQQEAELELEELKK-----KREERRKLLEEEE--------------------QRRKQEEAERKLREEEEKr 316
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958748272 2338 KLQQELERQKEEDELKRKvKRPKPGPvAKEEPPLKksqgPTNKQLPSVaKLEMKMESIERKV 2399
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 ...
2254-2368 1.05e-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: 51.05  E-value: 1.05e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272  2254 IYVINMSQDYVAMKAQEKAKKELEET--KRQEALAKEKERLQTLdEEEYDA----LTAEQkiafdREVRQALRERKKREL 2327
Cdd:smart00935    1 IGVVDVQKILQESPAGKAAQKQLEKEfkKRQAELEKLEKELQKL-KEKLQKdaatLSEAA-----REKKEKELQKKVQEF 74
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1958748272  2328 ERLAREMHEK--KLQQElERQKEEDELKRKVKRpkpgpVAKEE 2368
Cdd:smart00935   75 QRKQQKLQQDlqKRQQE-ELQKILDKINKAIKE-----VAKKK 111
PTZ00121 PTZ00121
MAEBL; Provisional
2265-2416 1.13e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.53  E-value: 1.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2265 AMKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRE-RKKRELERLAREMHEKKLQQEL 2343
Cdd:PTZ00121  1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKaEEAKKAEEAKKKAEEAKKADEA 1475
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958748272 2344 ERQKEE----DELKRKVKRPKpgpvAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKA 2416
Cdd:PTZ00121  1476 KKKAEEakkaDEAKKKAEEAK----KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
2266-2349 1.23e-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: 50.30  E-value: 1.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2266 MKAQEKAKKELEEtKRQEALAkEKERLqtldeEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELER 2345
Cdd:pfam20492   43 RRQAEEEAERLEQ-KRQEAEE-EKERL-----EESAEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEE 115

                   ....
gi 1958748272 2346 QKEE 2349
Cdd:pfam20492  116 AREE 119
PTZ00121 PTZ00121
MAEBL; Provisional
2265-2416 1.29e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.53  E-value: 1.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2265 AMKAQEKAKKELEETKRQE------ALAKEKERLQTLDEEEYDALTAEQKIAFDrEVRQALRERK---------KRELER 2329
Cdd:PTZ00121  1228 AVKKAEEAKKDAEEAKKAEeernneEIRKFEEARMAHFARRQAAIKAEEARKAD-ELKKAEEKKKadeakkaeeKKKADE 1306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2330 LAREMHEKKLQQELERQKEE-----DELKRKV-KRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKL---EMKMESIERKVS 2400
Cdd:PTZ00121  1307 AKKKAEEAKKADEAKKKAEEakkkaDAAKKKAeEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKkkeEAKKKADAAKKK 1386
                          170
                   ....*....|....*.
gi 1958748272 2401 VREHGLLEETtrKKKA 2416
Cdd:PTZ00121  1387 AEEKKKADEA--KKKA 1400
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
2289-2354 1.45e-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: 51.19  E-value: 1.45e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958748272 2289 KERLQTLDEEEYDALTAEQKiafdrevRQAlRERKKRE-LERLAREMHEKKLQQELERQKEEDELKR 2354
Cdd:pfam05672    1 KPSAGTTDAEEAARILAEKR-------RQA-REQREREeQERLEKEEEERLRKEELRRRAEEERARR 59
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
2264-2366 1.48e-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: 51.61  E-value: 1.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2264 VAMKAQEKAKKELEETKRQealaKEKERLQTLDEEEYDaltAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQEL 2343
Cdd:pfam11600   48 EKERAKEEARRKKEEEKEL----KEKERREKKEKDEKE---KAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEE 120
                           90       100
                   ....*....|....*....|....
gi 1958748272 2344 ERQK-EEDELKRKVKRPKPGPVAK 2366
Cdd:pfam11600  121 KRIKaEKAEITRFLQKPKTQQAPK 144
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
2265-2358 2.53e-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: 51.02  E-value: 2.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2265 AMKAQEKAKKELEETKRQ---EALAKEKERLQTLDEEEydaltaEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQ 2341
Cdd:cd23703     44 PLSEYQEWKRKMAELRRQnlrEGLRELEERKLKTEELR------AKRSERKQAERERALNAPEREDERLTLPTIESALLG 117
                           90       100
                   ....*....|....*....|..
gi 1958748272 2342 ELERQ-----KEEDELKRKVKR 2358
Cdd:cd23703    118 PLMRVrtdpeREERAAKRRANR 139
Caldesmon pfam02029
Caldesmon;
2274-2357 3.32e-06

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 53.33  E-value: 3.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2274 KELEETKRQEA---LAKEKERLQTLDEEEYDALTAEQkiafdREVRQALRE-RKKRELERLAREMHE-KKLQQELERQKE 2348
Cdd:pfam02029  236 REEEAEVFLEAeqkLEELRRRRQEKESEEFEKLRQKQ-----QEAELELEElKKKREERRKLLEEEEqRRKQEEAERKLR 310

                   ....*....
gi 1958748272 2349 EDELKRKVK 2357
Cdd:pfam02029  311 EEEEKRRMK 319
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2266-2358 3.47e-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: 52.61  E-value: 3.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2266 MKAQEKAKKELEETKRQEALAKEK--ERLQTLDEEEYdALTAEQKIAFDREVRQALRERKK-RELERLAREMHEKKLQQE 2342
Cdd:pfam13868   82 IEEREQKRQEEYEEKLQEREQMDEivERIQEEDQAEA-EEKLEKQRQLREEIDEFNEEQAEwKELEKEEEREEDERILEY 160
                           90
                   ....*....|....*.
gi 1958748272 2343 LeRQKEEDELKRKVKR 2358
Cdd:pfam13868  161 L-KEKAEREEEREAER 175
PTZ00121 PTZ00121
MAEBL; Provisional
2267-2416 3.48e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 3.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2267 KAQEKAKKElEETKRQEALAKEKERLQTLDEEEYDALTAEQKIafdREVRQALRERKKRELERLAREM----HEKKLQQE 2342
Cdd:PTZ00121  1386 KAEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKKADEAKKKA---EEKKKADEAKKKAEEAKKADEAkkkaEEAKKAEE 1461
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2343 LERQKEE----DELKRKVKRPKPGPVAKeepplKKSQGPTNK--QLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKA 2416
Cdd:PTZ00121  1462 AKKKAEEakkaDEAKKKAEEAKKADEAK-----KKAEEAKKKadEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
PTZ00121 PTZ00121
MAEBL; Provisional
2266-2416 3.95e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 3.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2266 MKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRE-RKKRELERLAREMHEKKLQQELE 2344
Cdd:PTZ00121  1410 LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKaEEAKKADEAKKKAEEAKKADEAK 1489
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958748272 2345 RQKEE-----DELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKA 2416
Cdd:PTZ00121  1490 KKAEEakkkaDEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2266-2463 4.10e-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: 53.44  E-value: 4.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2266 MKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEqkIAFDREVRQALRERKKRELERLAREMHE-KKLQQELE 2344
Cdd:pfam02463  254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE--EEELKSELLKLERRKVDDEEKLKESEKEkKKAEKELK 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2345 RQKEEDELKRKVKRPKPGPVAKEEppLKKSQgptnkqlpsvaklemkMESIERKVSVREHGLLEETTRKKKATTEYAfgf 2424
Cdd:pfam02463  332 KEKEEIEELEKELKELEIKREAEE--EEEEE----------------LEKLQEKLEQLEEELLAKKKLESERLSSAA--- 390
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1958748272 2425 pITQEQEESEGDFLKDSDKNLAQKFKVYDTCLKDVQNIL 2463
Cdd:pfam02463  391 -KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE 428
PTZ00121 PTZ00121
MAEBL; Provisional
2267-2414 5.66e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 5.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2267 KAQEKAKKELEETK-RQEALAK----EKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELErlaremhEKKLQQ 2341
Cdd:PTZ00121  1647 KKAEELKKAEEENKiKAAEEAKkaeeDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE-------EKKKAE 1719
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958748272 2342 ELERQKEE-----DELKRKVKRPKpgpvaKEEPPLKKSQGPTNKQLPSVAKLEMKMESIER-KVSVREHGLLEETTRKK 2414
Cdd:PTZ00121  1720 ELKKAEEEnkikaEEAKKEAEEDK-----KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKeKEAVIEEELDEEDEKRR 1793
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2264-2448 5.91e-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: 5.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2264 VAMKAQEKAKKELEETKrqEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQEL 2343
Cdd:COG1196    257 ELEAELAELEAELEELR--LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2344 ERQKEEDELKRKvkrpkpgpvAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKATTEyafg 2423
Cdd:COG1196    335 LEEELEELEEEL---------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ---- 401
                          170       180
                   ....*....|....*....|....*
gi 1958748272 2424 fpiTQEQEESEGDFLKDSDKNLAQK 2448
Cdd:COG1196    402 ---LEELEEAEEALLERLERLEEEL 423
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
2251-2361 7.08e-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: 48.33  E-value: 7.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2251 REhIYVINMSQDyvaMKAQEKAKKELEETKRQEALAKEKERLQTlDEEEYDALTAEQkiafDREVRQALRERKKRELERL 2330
Cdd:pfam13863    6 RE-MFLVQLALD---AKREEIERLEELLKQREEELEKKEQELKE-DLIKFDKFLKEN----DAKRRRALKKAEEETKLKK 76
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958748272 2331 AREMHEKKLQQELER-QKEEDELKRKVKRPKP 2361
Cdd:pfam13863   77 EKEKEIKKLTAQIEElKSEISKLEEKLEEYKP 108
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
2240-2419 7.26e-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: 7.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2240 ALICLLkAIGSREHIYVINMSQDYVAMKA----QEKAKKELEETKRQEALAKEKERlQTLDEEEYDALTAEQKIAFDREV 2315
Cdd:TIGR02794   13 LLLGLL-ILGSLYHSVKPEPGGGAEIIQAvlvdPGAVAQQANRIQQQKKPAAKKEQ-ERQKKLEQQAEEAEKQRAAEQAR 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2316 RQALRERKKRELErlAREMhEKKLQQELERQKEEDELKRKvkrPKPGPVAKEEPPL-KKSQGPTNKQLPSVAKLEMKMES 2394
Cdd:TIGR02794   91 QKELEQRAAAEKA--AKQA-EQAAKQAEEKQKQAEEAKAK---QAAEAKAKAEAEAeRKAKEEAAKQAEEEAKAKAAAEA 164
                          170       180
                   ....*....|....*....|....*
gi 1958748272 2395 ierKVSVREHGLLEETTRKKKATTE 2419
Cdd:TIGR02794  165 ---KKKAEEAKKKAEAEAKAKAEAE 186
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
2261-2355 8.19e-06

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: 48.89  E-value: 8.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2261 QDYVAMKAQEKAKKELEET--KRQEALAKEkerLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELErlaremhEKK 2338
Cdd:pfam15346    9 EEETARRVEEAVAKRVEEEleKRKDEIEAE---VERRVEEARKIMEKQVLEELEREREAELEEERRKEEE-------ERK 78
                           90       100
                   ....*....|....*....|..
gi 1958748272 2339 LQQELER-----QKEEDELKRK 2355
Cdd:pfam15346   79 KREELERileenNRKIEEAQRK 100
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
2253-2416 1.14e-05

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: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2253 HIYVINMSQDYVAMKAQEKAKKEleetkrqEALAKEKERLQTLDEEEYDALtaEQKIAFDREvrqALRERKKRELERLAR 2332
Cdd:pfam09731  293 HREIDQLSKKLAELKKREEKHIE-------RALEKQKEELDKLAEELSARL--EEVRAADEA---QLRLEFEREREEIRE 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2333 EMhEKKLQQELERQKE-------------EDELKRKVKRPKPGPVAKEEpplkksqgptNKQLPSVAKLEMKMESIERKV 2399
Cdd:pfam09731  361 SY-EEKLRTELERQAEaheehlkdvlveqEIELQREFLQDIKEKVEEER----------AGRLLKLNELLANLKGLEKAT 429
                          170
                   ....*....|....*..
gi 1958748272 2400 SvrEHGLLEETTRKKKA 2416
Cdd:pfam09731  430 S--SHSEVEDENRKAQQ 444
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
2254-2368 1.36e-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: 47.96  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2254 IYVINMSQDYVAMKAQEKAKKELEE--TKRQEALAKEKERLQTLdeeeYDALTAEQKIAfdrevrQALRERKKRELERLA 2331
Cdd:pfam03938    2 IGYVDMQKILEESPEGKAAQAQLEKkfKKRQAELEAKQKELQKL----YEELQKDGALL------EEEREEKEQELQKKE 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1958748272 2332 REMHE--KKLQQELERQKEE------DELKRKVKRpkpgpVAKEE 2368
Cdd:pfam03938   72 QELQQlqQKAQQELQKKQQEllqpiqDKINKAIKE-----VAKEK 111
Caldesmon pfam02029
Caldesmon;
2272-2438 1.70e-05

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 51.02  E-value: 1.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2272 AKKELEETKR-QEALAKEKERLQTL-DEEEYDALTAE--QKIAFDREVRQALRER-----KKRELERLAREMHEKKLQQE 2342
Cdd:pfam02029   69 AKREERRQKRlQEALERQKEFDPTIaDEKESVAERKEnnEEEENSSWEKEEKRDSrlgryKEEETEIREKEYQENKWSTE 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2343 LERQKE---EDELKRKVKRPKPGPV-AKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREhgllEETTRKKKATT 2418
Cdd:pfam02029  149 VRQAEEegeEEEDKSEEAEEVPTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGE----EEVTKLKVTTK 224
                          170       180
                   ....*....|....*....|
gi 1958748272 2419 EYAFGFPITQEQEESEGDFL 2438
Cdd:pfam02029  225 RRQGGLSQSQEREEEAEVFL 244
PRK12704 PRK12704
phosphodiesterase; Provisional
2267-2398 2.36e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 50.55  E-value: 2.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2267 KAQEKAKKELEETKRQ-EALAKEKErLQTldEEEYDALTAEqkiaFDREVRQalrerKKRELERLaremhEKKLQQELER 2345
Cdd:PRK12704    35 EAEEEAKRILEEAKKEaEAIKKEAL-LEA--KEEIHKLRNE----FEKELRE-----RRNELQKL-----EKRLLQKEEN 97
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958748272 2346 QKEEDELkrkvkrpkpgpVAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERK 2398
Cdd:PRK12704    98 LDRKLEL-----------LEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2265-2354 2.74e-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: 49.92  E-value: 2.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2265 AMKAQEKAKKElEETKRQEALAK---EKERLQTLDEEEYDaLTAEQKIAFDREVR---QALRERKKRELERLAREM---- 2334
Cdd:pfam13868   59 EEEEKEEERKE-ERKRYRQELEEqieEREQKRQEEYEEKL-QEREQMDEIVERIQeedQAEAEEKLEKQRQLREEIdefn 136
                           90       100
                   ....*....|....*....|
gi 1958748272 2335 HEKKLQQELERQKEEDELKR 2354
Cdd:pfam13868  137 EEQAEWKELEKEEEREEDER 156
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
2265-2357 2.85e-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: 49.59  E-value: 2.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2265 AMKAQEKAKKEleETKRQEALAKEKERLQTLDEEEyDALTAEQKIAFDREVRQaLRERKKRELERLAREmHEKKLQQELE 2344
Cdd:pfam02841  198 ALTAKEKAIEA--ERAKAEAAEAEQELLREKQKEE-EQMMEAQERSYQEHVKQ-LIEKMEAEREQLLAE-QERMLEHKLQ 272
                           90
                   ....*....|....*
gi 1958748272 2345 RQKE--EDELKRKVK 2357
Cdd:pfam02841  273 EQEEllKEGFKTEAE 287
PTZ00121 PTZ00121
MAEBL; Provisional
2248-2416 3.35e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 3.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2248 IGSREHIYVINMSQDYVAMKAQEKAK----KELEETKRQEALAKEKERlQTLDEEEYdalTAEQKIAFDREVRQAlrERK 2323
Cdd:PTZ00121  1254 IRKFEEARMAHFARRQAAIKAEEARKadelKKAEEKKKADEAKKAEEK-KKADEAKK---KAEEAKKADEAKKKA--EEA 1327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2324 KRELERLAREMHEKKLQQELERQKEE---DELKRKVKRPKPGPVAKEEPplKKSQGPTNKQLPSVAKL-EMKMESIERKV 2399
Cdd:PTZ00121  1328 KKKADAAKKKAEEAKKAAEAAKAEAEaaaDEAEAAEEKAEAAEKKKEEA--KKKADAAKKKAEEKKKAdEAKKKAEEDKK 1405
                          170
                   ....*....|....*..
gi 1958748272 2400 SVREhgLLEETTRKKKA 2416
Cdd:PTZ00121  1406 KADE--LKKAAAAKKKA 1420
Motile_Sperm pfam00635
MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These ...
227-302 3.67e-05

MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These proteins oligomerise to form filaments. This family contains many other proteins.


Pssm-ID: 459882  Cd Length: 109  Bit Score: 45.82  E-value: 3.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272  227 PDELNFSTCPVKYSTQKvLLVRNIGNKDSMFHLKTRSP--YSVEPTGGILNVGESMQLEVNFEPQTVG-----NHsgKLI 299
Cdd:pfam00635    7 PDLIFFAAPGNKQGTST-LTLKNTSDKRVAFKVKTTNPkkYRVRPNYGIIKPGESVTITITRQPFDEEpgdakKD--KFV 83

                   ...
gi 1958748272  300 VIY 302
Cdd:pfam00635   84 IQY 86
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
2270-2355 4.61e-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: 49.26  E-value: 4.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2270 EKAKKELEETKR-QEALAKEKER-LQTLDEEEYDAL-----TAEQKiafdREVRqALRERKKRELERLAREMHEKKLQQE 2342
Cdd:pfam15558  112 ERARQEAEQRKQcQEQRLKEKEEeLQALREQNSLQLqerleEACHK----RQLK-EREEQKKVQENNLSELLNHQARKVL 186
                           90
                   ....*....|....
gi 1958748272 2343 LERQ-KEEDELKRK 2355
Cdd:pfam15558  187 VDCQaKAEELLRRL 200
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2264-2358 5.05e-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: 5.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2264 VAMKAQEKAKKELEETKRQEALAKEKERL-----------QTLDE--EEYDALTAEQKIAFDREvRQALRERKKRELE-- 2328
Cdd:pfam13868   36 AEEKEEERRLDEMMEEERERALEEEEEKEeerkeerkryrQELEEqiEEREQKRQEEYEEKLQE-REQMDEIVERIQEed 114
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958748272 2329 -RLAREMHEKK--LQQELERQKEEDELKRKVKR 2358
Cdd:pfam13868  115 qAEAEEKLEKQrqLREEIDEFNEEQAEWKELEK 147
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2265-2358 5.23e-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: 5.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2265 AMKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERK-------KRELERLAREMHEK 2337
Cdd:pfam13868  226 EAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRrmkrlehRRELEKQIEEREEQ 305
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1958748272 2338 KL----------QQELERQKEEDELKRKVKR 2358
Cdd:pfam13868  306 RAaereeeleegERLREEEAERRERIEEERQ 336
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
2267-2360 5.38e-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: 48.73  E-value: 5.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2267 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQaLRERKKRELERLARE---MHEKKLQQEL 2343
Cdd:cd16269    191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQ-LKEKMEEERENLLKEqerALESKLKEQE 269
                           90       100
                   ....*....|....*....|..
gi 1958748272 2344 ERQKEE-----DELKRKVKRPK 2360
Cdd:cd16269    270 ALLEEGfkeqaELLQEEIRSLK 291
Cgr1 pfam03879
Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA ...
2260-2360 6.98e-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: 44.92  E-value: 6.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2260 SQDYVAMKAQEKAKKELEETKRQEALAKEKErLQTLDEEEydaltAEQKIAFDREvRQALRERKKReLERLAREMHEKKL 2339
Cdd:pfam03879   21 SSLVVGPKSKSWEKRQEKRLELKAIKAKEKE-LKDEKEAE-----RQRRIQAIKE-RREAKEEKER-YEELAAKMHAKKV 92
                           90       100
                   ....*....|....*....|.
gi 1958748272 2340 QQelerqkeedeLKRKVKRPK 2360
Cdd:pfam03879   93 ER----------LKRKEKRNK 103
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
2267-2418 7.30e-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: 7.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2267 KAQEKAKK-ELEETKRQEALAKEKERLQTldEEEYDALTAEQKIAfDREVRQALRERKKRELERLAREMHEKKLQQelER 2345
Cdd:COG3064     52 QAEEEAREaKAEAEQRAAELAAEAAKKLA--EAEKAAAEAEKKAA-AEKAKAAKEAEAAAAAEKAAAAAEKEKAEE--AK 126
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958748272 2346 QKEEDELKRKVKRPKPGpVAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKATT 2418
Cdd:COG3064    127 RKAEEEAKRKAEEERKA-AEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAA 198
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2267-2454 9.15e-05

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: 49.20  E-value: 9.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2267 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDaltaEQKIAFDREVRQALRERKKRELERLAREmhEKKLQQELERQ 2346
Cdd:pfam02463  201 KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLN----EERIDLLQELLRDEQEEIESSKQEIEKE--EEKLAQVLKEN 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2347 KEEdELKRKVKRPKPGPVAKEEppLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKAtTEYAFGFPI 2426
Cdd:pfam02463  275 KEE-EKEKKLQEEELKLLAKEE--EELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELE-KELKELEIK 350
                          170       180
                   ....*....|....*....|....*...
gi 1958748272 2427 TQEQEESEGDFLKDSDKNLAQKFKVYDT 2454
Cdd:pfam02463  351 REAEEEEEEELEKLQEKLEQLEEELLAK 378
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
2265-2369 9.68e-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: 9.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2265 AMKAQEKAKKELEETKRQEAlakEKERLQTLD-----EEEYDALTAEQKIAFDRevRQALRERKKRELERLAREMhEKKL 2339
Cdd:COG3064     20 QAEAEKRAAAEAEQKAKEEA---EEERLAELEakrqaEEEAREAKAEAEQRAAE--LAAEAAKKLAEAEKAAAEA-EKKA 93
                           90       100       110
                   ....*....|....*....|....*....|
gi 1958748272 2340 QQELERQKEEDElkRKVKRPKPGPVAKEEP 2369
Cdd:COG3064     94 AAEKAKAAKEAE--AAAAAEKAAAAAEKEK 121
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2270-2357 1.04e-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: 47.99  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2270 EKAKKELEETKRQEALAKEKERLQtlDEEEYDALtaEQKIAFDREVRQALRERKKRELERLAREmhekklqQELERQKEE 2349
Cdd:pfam13868  264 ERMLRKQAEDEEIEQEEAEKRRMK--RLEHRREL--EKQIEEREEQRAAEREEELEEGERLREE-------EAERRERIE 332

                   ....*...
gi 1958748272 2350 DELKRKVK 2357
Cdd:pfam13868  333 EERQKKLK 340
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
2267-2377 1.11e-04

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: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2267 KAQEKAKKELEETKRQ--------------EALAKEKERLQTLDEEEYDALTAEQKIafdrEVRQALRERKKRELERLAR 2332
Cdd:NF033838   315 EAKKKAKDQKEEDRRNyptntyktleleiaESDVKVKEAELELVKEEAKEPRNEEKI----KQAKAKVESKKAEATRLEK 390
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958748272 2333 EMHEKKLQQELERQK--EEDELKRK-VKRPKPGPVAKEEPPLKKSQGP 2377
Cdd:NF033838   391 IKTDRKKAEEEAKRKaaEEDKVKEKpAEQPQPAPAPQPEKPAPKPEKP 438
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2265-2453 1.15e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.97  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2265 AMKAQEKAKKELEETKRQ-----EALAKEKERLQTLdEEEYDALTAE-QKIAFDREVRQALRERKKRELERLAREMHEKK 2338
Cdd:COG4372     71 ARSELEQLEEELEELNEQlqaaqAELAQAQEELESL-QEEAEELQEElEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2339 LQ-QELERQKE--EDELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEET-TRKK 2414
Cdd:COG4372    150 EElKELEEQLEslQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKdSLEA 229
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1958748272 2415 KATTEYAFGFPITQEQEESEGDFLKDSDKNLAQKFKVYD 2453
Cdd:COG4372    230 KLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
2261-2416 1.26e-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: 48.11  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2261 QDYVAMKAQEKAKKELEetKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAR-----EMH 2335
Cdd:pfam15558   26 LQQQAALAWEELRRRDQ--KRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRwreqaEDQ 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2336 EKKLQQELERQKEEDELKRK--VKRPKpgpvAKEEppLKKSQGPTNKQLpsvakLEMKMESIERKVSVREHGL---LEET 2410
Cdd:pfam15558  104 ENQRQEKLERARQEAEQRKQcqEQRLK----EKEE--ELQALREQNSLQ-----LQERLEEACHKRQLKEREEqkkVQEN 172

                   ....*.
gi 1958748272 2411 TRKKKA 2416
Cdd:pfam15558  173 NLSELL 178
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2251-2358 1.38e-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: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2251 REHIYVINMSQDYVAMKAQEKAKKELEETkrQEALAKEKERLQTLdEEEYDALTAEQkiafdREVRQALRERKKRELERL 2330
Cdd:COG4913    272 AELEYLRAALRLWFAQRRLELLEAELEEL--RAELARLEAELERL-EARLDALREEL-----DELEAQIRGNGGDRLEQL 343
                           90       100
                   ....*....|....*....|....*...
gi 1958748272 2331 AREMHEKKLQQElERQKEEDELKRKVKR 2358
Cdd:COG4913    344 EREIERLERELE-ERERRRARLEALLAA 370
YscO pfam07321
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ...
2263-2352 1.43e-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: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2263 YVAMKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDAlTAEQKIAFDREVRQALRERkKRELERLAreMHEKKLQQE 2342
Cdd:pfam07321   55 YAEIQGKLVLLKELEKVKQQVALLRENEADLEKQVAEARQ-QLEAEREALRQARQALAEA-RRAVEKFA--ELVRLVQAE 130
                           90
                   ....*....|...
gi 1958748272 2343 LERQ---KEEDEL 2352
Cdd:pfam07321  131 ELRQqerQEEQEL 143
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
2261-2492 1.54e-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: 48.43  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2261 QDYVAMKAQEKAKKELEETKRQEAlakekerlqtldEEEYDALTaeQKIAFDREVRQALRERK----------KRELERL 2330
Cdd:TIGR00618  424 GQLAHAKKQQELQQRYAELCAAAI------------TCTAQCEK--LEKIHLQESAQSLKEREqqlqtkeqihLQETRKK 489
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2331 AREMHEKKLQQELERqkeedELKRKVKRPKPGPVAKEEPPLkkSQGPTNKQLPSVAKLEMKMESIerkvsvrEHGLLEET 2410
Cdd:TIGR00618  490 AVVLARLLELQEEPC-----PLCGSCIHPNPARQDIDNPGP--LTRRMQRGEQTYAQLETSEEDV-------YHQLTSER 555
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2411 TRKKkatteyafgfpITQEQEESEgdflKDSDKNLAQKFKVYDTCLKDVQNI---LMYW------DRKQGMMVPHTGPDE 2481
Cdd:TIGR00618  556 KQRA-----------SLKEQMQEI----QQSFSILTQCDNRSKEDIPNLQNItvrLQDLteklseAEDMLACEQHALLRK 620
                          250
                   ....*....|.
gi 1958748272 2482 IPHEVDDQRQA 2492
Cdd:TIGR00618  621 LQPEQDLQDVR 631
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2270-2416 1.82e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2270 EKAKKELEETKRQeaLAKEKERLQTLdEEEYDALTAEQKiafdrEVRQALrERKKRELERLAREMheKKLQQELER-QKE 2348
Cdd:COG4372     62 EQLEEELEQARSE--LEQLEEELEEL-NEQLQAAQAELA-----QAQEEL-ESLQEEAEELQEEL--EELQKERQDlEQQ 130
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958748272 2349 EDELKRKVKRPKPGPVAKEEpplkksqgptnkQLpsvAKLEMKMESIERKVSVREHGLLEETTRKKKA 2416
Cdd:COG4372    131 RKQLEAQIAELQSEIAEREE------------EL---KELEEQLESLQEELAALEQELQALSEAEAEQ 183
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
2269-2446 1.99e-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: 47.86  E-value: 1.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2269 QEKAKKELEE-TKRQEALAKEKERLQtldeeeyDALTAEQKIAFDREVRQALRERKKRELERLAREMhEKKLQQELERQK 2347
Cdd:pfam01576   21 QQKAESELKElEKKHQQLCEEKNALQ-------EQLQAETELCAEAEEMRARLAARKQELEEILHEL-ESRLEEEEERSQ 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2348 EEDELKRKVKRpkpgPVAKEEPPLKKSQGPTNK-QLPSVAkLEMKMESIERKVSV---------REHGLLEEttRKKKAT 2417
Cdd:pfam01576   93 QLQNEKKKMQQ----HIQDLEEQLDEEEAARQKlQLEKVT-TEAKIKKLEEDILLledqnsklsKERKLLEE--RISEFT 165
                          170       180
                   ....*....|....*....|....*....
gi 1958748272 2418 TEYAfgfpitqEQEESEGDFLKDSDKNLA 2446
Cdd:pfam01576  166 SNLA-------EEEEKAKSLSKLKNKHEA 187
Saf4_Yju2 pfam04502
Saf4/Yju2 protein; This is a family of eukaryotic proteins that includes CCDC130 and CCDC94 ...
2265-2448 2.73e-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: 46.58  E-value: 2.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2265 AMKAQEK----AKKELEETKRQEALAKEKERLQTLDeeeYDALtaeqkiafdREVRQALR-ERKKRELERLAREMHEKKL 2339
Cdd:pfam04502  130 AMKKLEKrtkdSKREMEALERLEELQELNQRQWKDD---YDAN---------LKLRREFReEKKEREEEEEDEEALKEKM 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2340 QQE-LERQKEEDELKRKVK------------RPKPGPVAKEEPPLKKSQGPTNKqlpsVAKLEMKMESIERKVSVREHGL 2406
Cdd:pfam04502  198 SLEiIKLLPEDEEDDRRAAlvefgsrplfgdSSPPAKTESPTDSLTSEISASSK----RESLKKSLGKLTRKAADPLLLG 273
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958748272 2407 LeetTRKKKATTEYAFGFPITQEQEESEGDFLKDSDKNLAQK 2448
Cdd:pfam04502  274 V---KRKKAATEEPSTPSSETSTESSKTSTPSSAQVSSSSPA 312
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
2265-2419 2.87e-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: 2.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2265 AMKAQEKAKKELEETKRQEALAKEKERLQtldeeeydaltAEQKIAFDREVRQAlRERKKRELERLAremhEKKLQQELE 2344
Cdd:COG3064     75 AAKKLAEAEKAAAEAEKKAAAEKAKAAKE-----------AEAAAAAEKAAAAA-EKEKAEEAKRKA----EEEAKRKAE 138
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958748272 2345 RQKEEDELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKATTE 2419
Cdd:COG3064    139 EERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
2270-2358 3.51e-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: 45.69  E-value: 3.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2270 EKAKKELEETKRQEALAKEKERLQTL-DEEEYDALTAEqkIAFDREVRQALRERKKRELERLarEMHEKKLQQ-ELERQK 2347
Cdd:COG1579     60 EIKRLELEIEEVEARIKKYEEQLGNVrNNKEYEALQKE--IESLKRRISDLEDEILELMERI--EELEEELAElEAELAE 135
                           90
                   ....*....|.
gi 1958748272 2348 EEDELKRKVKR 2358
Cdd:COG1579    136 LEAELEEKKAE 146
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
2270-2358 4.96e-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: 42.98  E-value: 4.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2270 EKAKKELEE---------TKRQEALAKEKERLQTLDEEEYDAltaeqkiafdREVRQALrERKKRELERLAREMHEKKLQ 2340
Cdd:pfam20492    5 EREKQELEErlkqyeeetKKAQEELEESEETAEELEEERRQA----------EEEAERL-EQKRQEAEEEKERLEESAEM 73
                           90       100
                   ....*....|....*....|.
gi 1958748272 2341 QELERQKEEDEL---KRKVKR 2358
Cdd:pfam20492   74 EAEEKEQLEAELaeaQEEIAR 94
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
2265-2350 5.30e-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: 43.63  E-value: 5.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2265 AMKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDA--LTAEQKiAFDREVRQALR-----ERKKREL-------ERL 2330
Cdd:pfam15236   54 ALEHQNAIKKQLEEKERQKKLEEERRRQEEQEEEERLRreREEEQK-QFEEERRKQKEkeeamTRKTQALlqamqkaQEL 132
                           90       100
                   ....*....|....*....|
gi 1958748272 2331 AREMHEKKLQQELErQKEED 2350
Cdd:pfam15236  133 AQRLKQEQRIRELA-EKGHD 151
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
2223-2377 7.41e-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: 7.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2223 GVVFDGLDTLFARNAPSALIcllkaigSRehIYVIN--MSQDYVAMKAQEKAKKELEETKrqEALAKEKERLQTL-DEEE 2299
Cdd:COG3883     99 GGSVSYLDVLLGSESFSDFL-------DR--LSALSkiADADADLLEELKADKAELEAKK--AELEAKLAELEALkAELE 167
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958748272 2300 YDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELERQKEEDELKRKVKRPKPGPVAKEEPPLKKSQGP 2377
Cdd:COG3883    168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
2266-2375 7.47e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.97  E-value: 7.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2266 MKAQEKAK---KELEETKR-QEALAKEKERLQtldeEEYDALTAEQKiafdREVRQALRERKKrELERLAREMHEK-KLQ 2340
Cdd:PRK00409   530 RELEQKAEeaeALLKEAEKlKEELEEKKEKLQ----EEEDKLLEEAE----KEAQQAIKEAKK-EADEIIKELRQLqKGG 600
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958748272 2341 QELERQKEEDELKRKVKRPKPgpvAKEEPPLKKSQ 2375
Cdd:PRK00409   601 YASVKAHELIEARKRLNKANE---KKEKKKKKQKE 632
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
2203-2259 8.16e-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: 8.16e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2203 PDDLLIQILAERIQLSDCFRGVVFDGldtlFARNAPSALIclLKAIGSREHI---YVINM 2259
Cdd:COG0563     60 PDEIVIGLVKERLAQPDCANGFILDG----FPRTVAQAEA--LDELLAELGIkldAVIEL 113
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
2261-2358 9.34e-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: 9.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2261 QDYVAMKAQEKAKKELEETKR-----------QEALAKEKERlQTLDEEEYDALTAEQKIAFDREVRQALRERKKREL-E 2328
Cdd:pfam15558  148 QERLEEACHKRQLKEREEQKKvqennlsellnHQARKVLVDC-QAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELrE 226
                           90       100       110
                   ....*....|....*....|....*....|
gi 1958748272 2329 RLAREmhEKKLQQELERQKEEDELKRKVKR 2358
Cdd:pfam15558  227 KAQKE--EEQFQRAKWRAEEKEEERQEHKE 254
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
2296-2421 1.15e-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: 44.15  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2296 DEEEYDALTAEQKIafDREVRQALRERKK--RELERLAREMheKKLQQELERQKEE-DELKRKVKRpKPGPVAKEEPPLK 2372
Cdd:COG1579      2 MPEDLRALLDLQEL--DSELDRLEHRLKElpAELAELEDEL--AALEARLEAAKTElEDLEKEIKR-LELEIEEVEARIK 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958748272 2373 KSQgptnKQLPSVAK------LEMKMESIERKVSVREHGLLEETTRKKKATTEYA 2421
Cdd:COG1579     77 KYE----EQLGNVRNnkeyeaLQKEIESLKRRISDLEDEILELMERIEELEEELA 127
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2273-2536 1.34e-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: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2273 KKELEETKRQEALAK-EKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKR---ELERLAREMhekklQQELERQKE 2348
Cdd:pfam17380  281 QKAVSERQQQEKFEKmEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyaEQERMAMER-----ERELERIRQ 355
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2349 EDElKRKVKRPKPGPVAKEeppLKKSQGPTNKQLPSVAKLEMKMESIErkvSVREHGLLEETtRKKKATTEYAFGFPITQ 2428
Cdd:pfam17380  356 EER-KRELERIRQEEIAME---ISRMRELERLQMERQQKNERVRQELE---AARKVKILEEE-RQRKIQQQKVEMEQIRA 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2429 EQEESEGDFLKDSDKNLAQKfkvydtclkdvqnilMYWDRKQGMmvphtgpdEIPHEVDDQRQAPSGGGGRKGRKDRERe 2508
Cdd:pfam17380  428 EQEEARQREVRRLEEERARE---------------MERVRLEEQ--------ERQQQVERLRQQEEERKRKKLELEKEK- 483
                          250       260
                   ....*....|....*....|....*...
gi 1958748272 2509 rleKERAEKERLEREKAERERLEKLRAM 2536
Cdd:pfam17380  484 ---RDRKRAEEQRRKILEKELEERKQAM 508
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
2271-2373 1.42e-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: 41.78  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2271 KAKKELEetkrQEALAKEKERLQTLDEEeydaltaEQKIAFDREVRQALRERKKRELERLAREMHEK--KLQQELERQKE 2348
Cdd:pfam00992   11 KAAEELE----FEQEKKEEEKLRYLAER-------IPPLRLRGLSAEQLQELCEELHERIDKLEEERydIEEKVAKKDKE 79
                           90       100
                   ....*....|....*....|....*..
gi 1958748272 2349 EDELKRKV--KRPKPGPvakeePPLKK 2373
Cdd:pfam00992   80 INDLKKKVndLRGKFKK-----PLLKK 101
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2267-2358 1.48e-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: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2267 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELERQ 2346
Cdd:COG1196    666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
                           90       100
                   ....*....|....*....|....*.
gi 1958748272 2347 KE--------------EDELKRKVKR 2358
Cdd:COG1196    746 ELleeealeelpeppdLEELERELER 771
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
2266-2357 1.77e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.41  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2266 MKAQEKAK-KELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELE 2344
Cdd:PRK09510   103 LKQLEKERlAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE 182
                           90
                   ....*....|....
gi 1958748272 2345 RQKE-EDELKRKVK 2357
Cdd:PRK09510   183 AKKKaEAEAAAKAA 196
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2264-2358 1.94e-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: 1.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2264 VAMKAQEKaKKELEETKRQEALAKEKERLQTLD--EEEYDALTAE-QKIAFDREVRQALRERKKRELERLAREMHEKKlQ 2340
Cdd:COG1196    211 KAERYREL-KEELKELEAELLLLKLRELEAELEelEAELEELEAElEELEAELAELEAELEELRLELEELELELEEAQ-A 288
                           90
                   ....*....|....*...
gi 1958748272 2341 QELERQKEEDELKRKVKR 2358
Cdd:COG1196    289 EEYELLAELARLEQDIAR 306
adk PRK00279
adenylate kinase; Reviewed
2203-2259 2.23e-03

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 42.83  E-value: 2.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958748272 2203 PDDLLIQILAERIQLSDCFRGVVFDGldtlFARNAP--SALICLLKAIGsREHIYVINM 2259
Cdd:PRK00279    60 PDEIVIGLVKERLAQPDCKNGFLLDG----FPRTIPqaEALDEMLKELG-IKLDAVIEI 113
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2265-2354 2.29e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2265 AMKAQEKAKKELEETKRQEALAKEKERLQTLDE-----EEYDALTAEQkiafdREVRQALrERKKRELERLAREMheKKL 2339
Cdd:COG4717    161 LEEELEELEAELAELQEELEELLEQLSLATEEElqdlaEELEELQQRL-----AELEEEL-EEAQEELEELEEEL--EQL 232
                           90
                   ....*....|....*
gi 1958748272 2340 QQELERQKEEDELKR 2354
Cdd:COG4717    233 ENELEAAALEERLKE 247
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2269-2358 2.37e-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: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2269 QEKAKKELEETKRQ-EALAKEKERLQTLDEEEYDALTAEQKiafDREVRQALRERKKRELERLAREM-HEKKLQQELERQ 2346
Cdd:COG1196    241 LEELEAELEELEAElEELEAELAELEAELEELRLELEELEL---ELEEAQAEEYELLAELARLEQDIaRLEERRRELEER 317
                           90
                   ....*....|..
gi 1958748272 2347 KEEDELKRKVKR 2358
Cdd:COG1196    318 LEELEEELAELE 329
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2244-2448 2.81e-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: 44.19  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2244 LLKAIG-SREHIYVINMSQDY--VAMKAQEKAKKELEETKRQEALAKEKERLQTLDEEeydALTAEQKIAFDREVRQALR 2320
Cdd:pfam02463  124 LLESQGiSPEAYNFLVQGGKIeiIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEE---TENLAELIIDLEELKLQEL 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2321 ERKKRELERLAREMHEKKLQQELERQKEEDELKRKVKRpkpgpvakeeppLKKSQGPTNKQLPSVAKLEMKMESIERKvS 2400
Cdd:pfam02463  201 KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER------------IDLLQELLRDEQEEIESSKQEIEKEEEK-L 267
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958748272 2401 VREHGLLEETTRKKKATTEYAfGFPITQEQEESEGDFLKDSDKNLAQK 2448
Cdd:pfam02463  268 AQVLKENKEEEKEKKLQEEEL-KLLAKEEEELKSELLKLERRKVDDEE 314
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
2267-2352 4.14e-03

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 442129 [Multi-domain]  Cd Length: 142  Bit Score: 40.66  E-value: 4.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2267 KAQEKAKKELeeTKRQEALAKEKERLQTLDE--EEY---------------------------DALTAEQKIAFDR---- 2313
Cdd:COG2882     16 KEEDEAAREL--GQAQQALEQAEEQLEQLEQyrEEYeqrlqqklqqglsaaqlrnyqqfiarlDEAIEQQQQQVAQaeqq 93
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1958748272 2314 --EVRQALRERKKRE--LERLaREMHEKKLQQELER--QKEEDEL 2352
Cdd:COG2882     94 veQARQAWLEARQERkaLEKL-KERRREEERQEENRreQKELDEL 137
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2265-2349 4.46e-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: 4.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2265 AMKAQEKAKKELEETKRQeaLAKEKERLQTLDEEEYDAL----TAEQKIAFDREVRQALRER---KKRELERLAREmhEK 2337
Cdd:COG4942     18 QADAAAEAEAELEQLQQE--IAELEKELAALKKEEKALLkqlaALERRIAALARRIRALEQElaaLEAELAELEKE--IA 93
                           90
                   ....*....|..
gi 1958748272 2338 KLQQELERQKEE 2349
Cdd:COG4942     94 ELRAELEAQKEE 105
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2270-2414 4.76e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 4.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2270 EKAKKELEE-TKRQEALAKEKERLQTLDEEEYDALTAEQKI----AFDREVRQALRER------KKRELERLAREmhEKK 2338
Cdd:PRK03918   272 KKEIEELEEkVKELKELKEKAEEYIKLSEFYEEYLDELREIekrlSRLEEEINGIEERikeleeKEERLEELKKK--LKE 349
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958748272 2339 LQQELERQKEEDELKRKVKRPKpgpvaKEEPPLKKSQGPTNKQlpsvaKLEMKMESIE-RKVSVREHglLEETTRKK 2414
Cdd:PRK03918   350 LEKRLEELEERHELYEEAKAKK-----EELERLKKRLTGLTPE-----KLEKELEELEkAKEEIEEE--ISKITARI 414
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2267-2358 5.24e-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: 5.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2267 KAQEKAKKELEE-TKRQEALakekERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKrELERLAREmhEKKLQQELER 2345
Cdd:COG4913    631 ERLEALEAELDAlQERREAL----QRLAEYSWDEIDVASAEREIAELEAELERLDASSD-DLAALEEQ--LEELEAELEE 703
                           90
                   ....*....|....
gi 1958748272 2346 QKEE-DELKRKVKR 2358
Cdd:COG4913    704 LEEElDELKGEIGR 717
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2266-2376 6.61e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 6.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2266 MKAQEKAKKELEE-TKRQEALAKEKERLQTlDEEEYDalTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELE 2344
Cdd:PRK03918   330 IKELEEKEERLEElKKKLKELEKRLEELEE-RHELYE--EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEE 406
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958748272 2345 RQKEED---ELKRKVKRPKPgpvAKEEppLKKSQG 2376
Cdd:PRK03918   407 ISKITArigELKKEIKELKK---AIEE--LKKAKG 436
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2267-2355 7.40e-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: 7.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2267 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELERQ 2346
Cdd:COG1196    366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445

                   ....*....
gi 1958748272 2347 KEEDELKRK 2355
Cdd:COG1196    446 EAAEEEAEL 454
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
2306-2431 8.75e-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: 41.07  E-value: 8.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272 2306 EQKI-AFDREVRQALRERKKR---------ELERLAREMHEKKLQqeLERQKEEDELKRKVKrpkpgpvAKEE--PPLKK 2373
Cdd:pfam06391   67 EKKIeQYEKENKDLILKNKMKlsqeeeeleELLELEKREKEERRK--EEKQEEEEEKEKKEK-------AKQEliDELMT 137
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958748272 2374 SQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKATTEYAFGFPITQEQE 2431
Cdd:pfam06391  138 SNKDAEEIIAQHKKTAKKRKSERRRKLEELNRVLEQKPTQFSTGIKFGQLPVPKIEEG 195
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
2270-2355 8.77e-03

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


Pssm-ID: 128778  Cd Length: 127  Bit Score: 39.56  E-value: 8.77e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748272  2270 EKAKKELEETKRqeALAKEKERLQTLdEEEYDALTAEQKIAFDrEVRQALRERKKRELERL--AREMHEKKLQQELER-Q 2346
Cdd:smart00502   10 TKLRKKAAELED--ALKQLISIIQEV-EENAADVEAQIKAAFD-ELRNALNKRKKQLLEDLeeQKENKLKVLEQQLESlT 85

                    ....*....
gi 1958748272  2347 KEEDELKRK 2355
Cdd:smart00502   86 QKQEKLSHA 94
 
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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