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Conserved domains on  [gi|1958748270|ref|XP_038954162|]
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hydrocephalus-inducing protein homolog isoform X2 [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 ...
2044-2268 6.91e-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: 6.91e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2044 AIIVYGTPVSGKTANAISMAKFYNTACLNIDSIVLEALSDSNNVLGIRARELCIRAAIEQSMREAEESAQESSVTQNLGA 2123
Cdd:pfam17213    1 AIIVHGAPLSGKTATAVTLAKHYGAACLTIDSIVLEAISDGNSIAGLRARELCARAAIEQSEREAEEAAQEAAVVPGQPT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2124 PARLSTENLGRFTSDLTLLTQEYKIPKSMRGSVMLSKGKTESHWSGSqkqqgqqqqqqqqqqpqqqqqpqqqqQQQHHQH 2203
Cdd:pfam17213   81 TYRLSVEALTKHTSEGTLVGPESKISKGKRGSVVSGKGKADSHGTGS--------------------------QKQHHQH 134
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958748270 2204 QSETPQISSSPLLGGPTQRRLSVSASIGGETGLMSCVLPDDLLIQILAERIQLSDCFRGVVFDGL 2268
Cdd:pfam17213  135 QSETPQISSSPPPAGPIQRRLSVSASVGGEEGLMSCVLPEDLLVEILAERIQLNDCHRGVVFDGL 199
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
531-630 3.28e-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: 3.28e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270  531 EGIIEPSGVQAvQIAFSSTSLGHFEEEFLIDVNGSPEPVkLTIRGCVIGPTFHFNVPALHFgNVSYGFPHTLTCSLNNTS 610
Cdd:pfam15780    2 VLLLAPFSRQP-FVCFGDVPVGTSAERLLTVVNPSEEPA-EVKVSKVPAPTKGFSVSPLEF-TVQPGESQTLTVTWTPTE 78
                           90       100
                   ....*....|....*....|
gi 1958748270  611 LVSMTFKLRVRGDGEGMSSI 630
Cdd:pfam15780   79 EGAVRETLQFTVNDVGKHQV 98
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2306-2453 3.34e-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: 3.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2306 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQaLRERKKRELERLAREMHEKKLQQELERQ 2385
Cdd:pfam17380  389 QKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR-LEEERAREMERVRLEEQERQQQVERLRQ 467
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958748270 2386 KEEDELKRKVKRPKPGPVAKEEPPLKK----SQGPTNKQlpSVAKLEMKMESIERKVSVREHGLLEETTRKK 2453
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 3.66e-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: 3.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270  227 PDELNFSTCPVKYSTQKvLLVRNIGNKDSMFHLKTRSP--YSVEPTGGILNVGESMQLEVNFEPQTVG-----NHsgKLI 299
Cdd:pfam00635    7 PDLIFFAAPGNKQGTST-LTLKNTSDKRVAFKVKTTNPkkYRVRPNYGIIKPGESVTITITRQPFDEEpgdakKD--KFV 83

                   ...
gi 1958748270  300 VIY 302
Cdd:pfam00635   84 IQY 86
Adk super family cl33950
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
2242-2298 8.22e-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: 8.22e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2242 PDDLLIQILAERIQLSDCFRGVVFDGldtlFARNAPSALIclLKAIGSREHI---YVINM 2298
Cdd:COG0563     60 PDEIVIGLVKERLAQPDCANGFILDG----FPRTVAQAEA--LDELLAELGIkldAVIEL 113
PTZ00121 super family cl31754
MAEBL; Provisional
2304-2609 9.95e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 9.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2304 AMKAQEKAK----KELEETKRQEAL--AKEKERLQTLDEEEyDALTAEQKiafdREVRQALR--ERKKRELER--LAREM 2373
Cdd:PTZ00121  1515 AKKAEEAKKadeaKKAEEAKKADEAkkAEEKKKADELKKAE-ELKKAEEK----KKAEEAKKaeEDKNMALRKaeEAKKA 1589
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2374 HEK------KLQQELERQKEEDELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLE-MKMESIERKVSVREHGLL 2446
Cdd:PTZ00121  1590 EEArieevmKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEeLKKAEEENKIKAAEEAKK 1669
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2447 EETTRKKKATTEYAfgfpitQEQEESEGDFLKdsdKNLAQKFKVYDTCLKDVQNILMYWDRKQGMMVPHTGPDEIPHEVD 2526
Cdd:PTZ00121  1670 AEEDKKKAEEAKKA------EEDEKKAAEALK---KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2527 -DQRQAPSGGGGRKGRKDRERErlekeraekERLEREKAERERLEKLRAMEERSDGEGEGEEEHEGK--KDLGVPFINIQ 2603
Cdd:PTZ00121  1741 eDKKKAEEAKKDEEEKKKIAHL---------KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKkiKDIFDNFANII 1811

                   ....*.
gi 1958748270 2604 TPDFEG 2609
Cdd:PTZ00121  1812 EGGKEG 1817
 
Name Accession Description Interval E-value
Hydin_ADK pfam17213
Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to ...
2044-2268 6.91e-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: 6.91e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2044 AIIVYGTPVSGKTANAISMAKFYNTACLNIDSIVLEALSDSNNVLGIRARELCIRAAIEQSMREAEESAQESSVTQNLGA 2123
Cdd:pfam17213    1 AIIVHGAPLSGKTATAVTLAKHYGAACLTIDSIVLEAISDGNSIAGLRARELCARAAIEQSEREAEEAAQEAAVVPGQPT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2124 PARLSTENLGRFTSDLTLLTQEYKIPKSMRGSVMLSKGKTESHWSGSqkqqgqqqqqqqqqqpqqqqqpqqqqQQQHHQH 2203
Cdd:pfam17213   81 TYRLSVEALTKHTSEGTLVGPESKISKGKRGSVVSGKGKADSHGTGS--------------------------QKQHHQH 134
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958748270 2204 QSETPQISSSPLLGGPTQRRLSVSASIGGETGLMSCVLPDDLLIQILAERIQLSDCFRGVVFDGL 2268
Cdd:pfam17213  135 QSETPQISSSPPPAGPIQRRLSVSASVGGEEGLMSCVLPEDLLVEILAERIQLNDCHRGVVFDGL 199
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
531-630 3.28e-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: 3.28e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270  531 EGIIEPSGVQAvQIAFSSTSLGHFEEEFLIDVNGSPEPVkLTIRGCVIGPTFHFNVPALHFgNVSYGFPHTLTCSLNNTS 610
Cdd:pfam15780    2 VLLLAPFSRQP-FVCFGDVPVGTSAERLLTVVNPSEEPA-EVKVSKVPAPTKGFSVSPLEF-TVQPGESQTLTVTWTPTE 78
                           90       100
                   ....*....|....*....|
gi 1958748270  611 LVSMTFKLRVRGDGEGMSSI 630
Cdd:pfam15780   79 EGAVRETLQFTVNDVGKHQV 98
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2306-2453 3.34e-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: 3.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2306 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQaLRERKKRELERLAREMHEKKLQQELERQ 2385
Cdd:pfam17380  389 QKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR-LEEERAREMERVRLEEQERQQQVERLRQ 467
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958748270 2386 KEEDELKRKVKRPKPGPVAKEEPPLKK----SQGPTNKQlpSVAKLEMKMESIERKVSVREHGLLEETTRKK 2453
Cdd:pfam17380  468 QEEERKRKKLELEKEKRDRKRAEEQRRkileKELEERKQ--AMIEEERKRKLLEKEMEERQKAIYEEERRRE 537
PTZ00121 PTZ00121
MAEBL; Provisional
2284-2453 9.36e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 9.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2284 LKAIGSREHIYVINMSQDYVAMKAqEKAKKELEETKRQEALAKEkerlqtldeEEYDALTAEQKIAFDREVRQAlRERKK 2363
Cdd:PTZ00121  1586 AKKAEEARIEEVMKLYEEEKKMKA-EEAKKAEEAKIKAEELKKA---------EEEKKKVEQLKKKEAEEKKKA-EELKK 1654
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2364 RELERLAREMHEKKLQQELERQKEEDELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLE-MKMESIERKVSVRE 2442
Cdd:PTZ00121  1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEeLKKAEEENKIKAEE 1734
                          170
                   ....*....|.
gi 1958748270 2443 HGLLEETTRKK 2453
Cdd:PTZ00121  1735 AKKEAEEDKKK 1745
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
2306-2489 3.52e-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: 3.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2306 KAQEKAKKELEETKRQ--EALAKEKERLQTLDE---EEYDALTAEQ--KIAFDREvRQALRERKKRELERLARE--MHEK 2376
Cdd:TIGR02794   64 KKEQERQKKLEQQAEEaeKQRAAEQARQKELEQraaAEKAAKQAEQaaKQAEEKQ-KQAEEAKAKQAAEAKAKAeaEAER 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2377 KLQQELERQKEED-------ELKRKV----KRPKPGPVAKEEpPLKKSQGPTNKQLPSVAKLEMKMESIERKvsVREHGL 2445
Cdd:TIGR02794  143 KAKEEAAKQAEEEakakaaaEAKKKAeeakKKAEAEAKAKAE-AEAKAKAEEAKAKAEAAKAKAAAEAAAKA--EAEAAA 219
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2446 LEETTRKKKATTEYAFGFP------ITQEQEESEGDFLKDSDKNLAQKFK 2489
Cdd:TIGR02794  220 AAAAEAERKADEAELGDIFglasgsNAEKQGGARGAAAGSEVDKYAAIIQ 269
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
2307-2455 4.09e-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: 4.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2307 AQEKAKKELEETKRQEALAKEKERLQTLDEEEYDAL--TAEQKIAFDREVRQALRE--RKKRELERLAREMHEKKLQQEL 2382
Cdd:COG3064      1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKeeAEEERLAELEAKRQAEEEarEAKAEAEQRAAELAAEAAKKLA 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958748270 2383 ERQKEEDELKRKVKRPKPGPVAKEEPPLKKsqgptnKQLPSVAKLEmKMESIERKVsvrehglleETTRKKKA 2455
Cdd:COG3064     81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAA------EKAAAAAEKE-KAEEAKRKA---------EEEAKRKA 137
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
2293-2407 1.03e-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: 1.03e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270  2293 IYVINMSQDYVAMKAQEKAKKELEET--KRQEALAKEKERLQTLdEEEYDA----LTAEQkiafdREVRQALRERKKREL 2366
Cdd:smart00935    1 IGVVDVQKILQESPAGKAAQKQLEKEfkKRQAELEKLEKELQKL-KEKLQKdaatLSEAA-----REKKEKELQKKVQEF 74
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1958748270  2367 ERLAREMHEK--KLQQElERQKEEDELKRKVKRpkpgpVAKEE 2407
Cdd:smart00935   75 QRKQQKLQQDlqKRQQE-ELQKILDKINKAIKE-----VAKKK 111
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
2304-2397 2.57e-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: 2.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2304 AMKAQEKAKKELEETKRQ---EALAKEKERLQTLDEEEydaltaEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQ 2380
Cdd:cd23703     44 PLSEYQEWKRKMAELRRQnlrEGLRELEERKLKTEELR------AKRSERKQAERERALNAPEREDERLTLPTIESALLG 117
                           90       100
                   ....*....|....*....|..
gi 1958748270 2381 ELERQ-----KEEDELKRKVKR 2397
Cdd:cd23703    118 PLMRVrtdpeREERAAKRRANR 139
Motile_Sperm pfam00635
MSP (Major sperm protein) domain; Major sperm proteins are involved in sperm motility. These ...
227-302 3.66e-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: 3.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270  227 PDELNFSTCPVKYSTQKvLLVRNIGNKDSMFHLKTRSP--YSVEPTGGILNVGESMQLEVNFEPQTVG-----NHsgKLI 299
Cdd:pfam00635    7 PDLIFFAAPGNKQGTST-LTLKNTSDKRVAFKVKTTNPkkYRVRPNYGIIKPGESVTITITRQPFDEEpgdakKD--KFV 83

                   ...
gi 1958748270  300 VIY 302
Cdd:pfam00635   84 IQY 86
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
2306-2416 1.12e-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: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2306 KAQEKAKKELEETKRQ--------------EALAKEKERLQTLDEEEYDALTAEQKIafdrEVRQALRERKKRELERLAR 2371
Cdd:NF033838   315 EAKKKAKDQKEEDRRNyptntyktleleiaESDVKVKEAELELVKEEAKEPRNEEKI----KQAKAKVESKKAEATRLEK 390
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958748270 2372 EMHEKKLQQELERQK--EEDELKRK-VKRPKPGPVAKEEPPLKKSQGP 2416
Cdd:NF033838   391 IKTDRKKAEEEAKRKaaEEDKVKEKpAEQPQPAPAPQPEKPAPKPEKP 438
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
2242-2298 8.22e-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: 8.22e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2242 PDDLLIQILAERIQLSDCFRGVVFDGldtlFARNAPSALIclLKAIGSREHI---YVINM 2298
Cdd:COG0563     60 PDEIVIGLVKERLAQPDCANGFILDG----FPRTVAQAEA--LDELLAELGIkldAVIEL 113
adk PRK00279
adenylate kinase; Reviewed
2242-2298 2.25e-03

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 42.83  E-value: 2.25e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958748270 2242 PDDLLIQILAERIQLSDCFRGVVFDGldtlFARNAP--SALICLLKAIGsREHIYVINM 2298
Cdd:PRK00279    60 PDEIVIGLVKERLAQPDCKNGFLLDG----FPRTIPqaEALDEMLKELG-IKLDAVIEI 113
PTZ00121 PTZ00121
MAEBL; Provisional
2304-2609 9.95e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 9.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2304 AMKAQEKAK----KELEETKRQEAL--AKEKERLQTLDEEEyDALTAEQKiafdREVRQALR--ERKKRELER--LAREM 2373
Cdd:PTZ00121  1515 AKKAEEAKKadeaKKAEEAKKADEAkkAEEKKKADELKKAE-ELKKAEEK----KKAEEAKKaeEDKNMALRKaeEAKKA 1589
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2374 HEK------KLQQELERQKEEDELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLE-MKMESIERKVSVREHGLL 2446
Cdd:PTZ00121  1590 EEArieevmKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEeLKKAEEENKIKAAEEAKK 1669
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2447 EETTRKKKATTEYAfgfpitQEQEESEGDFLKdsdKNLAQKFKVYDTCLKDVQNILMYWDRKQGMMVPHTGPDEIPHEVD 2526
Cdd:PTZ00121  1670 AEEDKKKAEEAKKA------EEDEKKAAEALK---KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2527 -DQRQAPSGGGGRKGRKDRERErlekeraekERLEREKAERERLEKLRAMEERSDGEGEGEEEHEGK--KDLGVPFINIQ 2603
Cdd:PTZ00121  1741 eDKKKAEEAKKDEEEKKKIAHL---------KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKkiKDIFDNFANII 1811

                   ....*.
gi 1958748270 2604 TPDFEG 2609
Cdd:PTZ00121  1812 EGGKEG 1817
 
Name Accession Description Interval E-value
Hydin_ADK pfam17213
Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to ...
2044-2268 6.91e-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: 6.91e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2044 AIIVYGTPVSGKTANAISMAKFYNTACLNIDSIVLEALSDSNNVLGIRARELCIRAAIEQSMREAEESAQESSVTQNLGA 2123
Cdd:pfam17213    1 AIIVHGAPLSGKTATAVTLAKHYGAACLTIDSIVLEAISDGNSIAGLRARELCARAAIEQSEREAEEAAQEAAVVPGQPT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2124 PARLSTENLGRFTSDLTLLTQEYKIPKSMRGSVMLSKGKTESHWSGSqkqqgqqqqqqqqqqpqqqqqpqqqqQQQHHQH 2203
Cdd:pfam17213   81 TYRLSVEALTKHTSEGTLVGPESKISKGKRGSVVSGKGKADSHGTGS--------------------------QKQHHQH 134
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958748270 2204 QSETPQISSSPLLGGPTQRRLSVSASIGGETGLMSCVLPDDLLIQILAERIQLSDCFRGVVFDGL 2268
Cdd:pfam17213  135 QSETPQISSSPPPAGPIQRRLSVSASVGGEEGLMSCVLPEDLLVEILAERIQLNDCHRGVVFDGL 199
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
531-630 3.28e-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: 3.28e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270  531 EGIIEPSGVQAvQIAFSSTSLGHFEEEFLIDVNGSPEPVkLTIRGCVIGPTFHFNVPALHFgNVSYGFPHTLTCSLNNTS 610
Cdd:pfam15780    2 VLLLAPFSRQP-FVCFGDVPVGTSAERLLTVVNPSEEPA-EVKVSKVPAPTKGFSVSPLEF-TVQPGESQTLTVTWTPTE 78
                           90       100
                   ....*....|....*....|
gi 1958748270  611 LVSMTFKLRVRGDGEGMSSI 630
Cdd:pfam15780   79 EGAVRETLQFTVNDVGKHQV 98
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2306-2453 3.34e-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: 3.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2306 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQaLRERKKRELERLAREMHEKKLQQELERQ 2385
Cdd:pfam17380  389 QKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR-LEEERAREMERVRLEEQERQQQVERLRQ 467
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958748270 2386 KEEDELKRKVKRPKPGPVAKEEPPLKK----SQGPTNKQlpSVAKLEMKMESIERKVSVREHGLLEETTRKK 2453
Cdd:pfam17380  468 QEEERKRKKLELEKEKRDRKRAEEQRRkileKELEERKQ--AMIEEERKRKLLEKEMEERQKAIYEEERRRE 537
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2305-2473 2.23e-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: 2.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2305 MKAQEKAKKELEETKRQEALAKEKERLQTLDEE----EYDALTAEQKIAFDREvRQALRERKKRELERLAR--------- 2371
Cdd:pfam13868  122 LEKQRQLREEIDEFNEEQAEWKELEKEEEREEDerilEYLKEKAEREEEREAE-REEIEEEKEREIARLRAqqekaqdek 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2372 ----EMHEKKLQQELE---RQKEEDELKRKVKRpkpgpvaKEEppLKKSQgptNKQLpsvaKLEMKMESIERKvsvREHG 2444
Cdd:pfam13868  201 aerdELRAKLYQEEQErkeRQKEREEAEKKARQ-------RQE--LQQAR---EEQI----ELKERRLAEEAE---REEE 261
                          170       180
                   ....*....|....*....|....*....
gi 1958748270 2445 LLEETTRKKKatteyafgFPITQEQEESE 2473
Cdd:pfam13868  262 EFERMLRKQA--------EDEEIEQEEAE 282
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
2308-2402 1.11e-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: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2308 QEKAKKELEETKRQEaLAKE--------KERLQTLDEEEYDALTAEQKIAFDR----------EVRQALRE--RKKRELE 2367
Cdd:pfam13904   77 EEREKEEQEAELRKR-LAKEkyqewlqrKARQQTKKREESHKQKAAESASKSLakperkvsqeEAKEVLQEweRKKLEQQ 155
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1958748270 2368 ---RLAREMHEKKLQQELERQKEEDELK-----RKVK-RPKPGP 2402
Cdd:pfam13904  156 qrkREEEQREQLKKEEEEQERKQLAEKAwqkwmKNVKnKPKPVP 199
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
2309-2397 1.47e-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: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2309 EKAKKELEE-TKRQEALAKEKERLQtldeEEYDALTAEQKIAfdREVRQALRERK---KRELERLAREMHEK-----KLQ 2379
Cdd:pfam20492   23 KKAQEELEEsEETAEELEEERRQAE----EEAERLEQKRQEA--EEEKERLEESAemeAEEKEQLEAELAEAqeeiaRLE 96
                           90
                   ....*....|....*....
gi 1958748270 2380 QELERQKEE-DELKRKVKR 2397
Cdd:pfam20492   97 EEVERKEEEaRRLQEELEE 115
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2300-2489 1.76e-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: 1.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2300 QDYVAMKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKK-L 2378
Cdd:pfam13868  158 LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQeL 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2379 QQELERQKEEDELKRKVKRpkpgpvAKEE----PPLKKSQGPTNKQLPSVAKLEMKMEsiERKVSVREhgLLEETTRKKK 2454
Cdd:pfam13868  238 QQAREEQIELKERRLAEEA------EREEeefeRMLRKQAEDEEIEQEEAEKRRMKRL--EHRRELEK--QIEEREEQRA 307
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1958748270 2455 AtteyafgfpiTQEQEESEGDFLKDSDKNLAQKFK 2489
Cdd:pfam13868  308 A----------EREEELEEGERLREEEAERRERIE 332
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
2309-2392 2.63e-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: 2.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2309 EKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAE---QKIAFDR-----EVRQALRERKKRELERLA--------RE 2372
Cdd:pfam05672   10 EEAARILAEKRRQAREQREREEQERLEKEEEERLRKEelrRRAEEERarreeEARRLEEERRREEEERQRkaeeeaeeRE 89
                           90       100
                   ....*....|....*....|
gi 1958748270 2373 MHEKKLQQELERQKEEDELK 2392
Cdd:pfam05672   90 QREQEEQERLQKQKEEAEAK 109
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2298-2573 2.80e-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: 2.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2298 MSQDYVAMKAQEKAK-----KELEETK--------RQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQ---ALRER 2361
Cdd:pfam17380  296 MEQERLRQEKEEKAReverrRKLEEAEkarqaemdRQAAIYAEQERMAMERERELERIRQEERKRELERIRQeeiAMEIS 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2362 KKRELERLAREMHEK--KLQQELE---RQK-EEDELKRKVKRPKpgpvaKEEPPLKKSQgpTNKQLPSVAKLE------- 2428
Cdd:pfam17380  376 RMRELERLQMERQQKneRVRQELEaarKVKiLEEERQRKIQQQK-----VEMEQIRAEQ--EEARQREVRRLEeerarem 448
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2429 --MKMESIERKVSVREHGLLEETTRKKKATTEYAfgfpiTQEQEESEgdflkdsdknlAQKFKVYDTCLKDVQNILMYWD 2506
Cdd:pfam17380  449 erVRLEEQERQQQVERLRQQEEERKRKKLELEKE-----KRDRKRAE-----------EQRRKILEKELEERKQAMIEEE 512
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958748270 2507 RKQGMMVPHTGPDEIP-HEVDDQRQAPSGGGGRKGRKDRERERLEKERAEKERLEREKAERERlEKLR 2573
Cdd:pfam17380  513 RKRKLLEKEMEERQKAiYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERER-EMMR 579
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2308-2397 6.34e-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: 6.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2308 QEKAKKELEETKRQEALAK--EKERLQTLD-EEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQE-LE 2383
Cdd:pfam13868   29 AEKKRIKAEEKEEERRLDEmmEEERERALEeEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEiVE 108
                           90
                   ....*....|....
gi 1958748270 2384 RQKEEDELKRKVKR 2397
Cdd:pfam13868  109 RIQEEDQAEAEEKL 122
PTZ00121 PTZ00121
MAEBL; Provisional
2284-2453 9.36e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 9.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2284 LKAIGSREHIYVINMSQDYVAMKAqEKAKKELEETKRQEALAKEkerlqtldeEEYDALTAEQKIAFDREVRQAlRERKK 2363
Cdd:PTZ00121  1586 AKKAEEARIEEVMKLYEEEKKMKA-EEAKKAEEAKIKAEELKKA---------EEEKKKVEQLKKKEAEEKKKA-EELKK 1654
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2364 RELERLAREMHEKKLQQELERQKEEDELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLE-MKMESIERKVSVRE 2442
Cdd:PTZ00121  1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEeLKKAEEENKIKAEE 1734
                          170
                   ....*....|.
gi 1958748270 2443 HGLLEETTRKK 2453
Cdd:PTZ00121  1735 AKKEAEEDKKK 1745
PTZ00121 PTZ00121
MAEBL; Provisional
2299-2458 1.51e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 1.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2299 SQDYVAMKAQEKAKKELEETKRQEALAKEKE----RLQTLDEEEYDALTAEQ-KIAFDREVRQALRERKKRE-----LER 2368
Cdd:PTZ00121  1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEdekkAAEALKKEAEEAKKAEElKKKEAEEKKKAEELKKAEEenkikAEE 1734
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2369 LAREMHEKKLQQElERQKEEDElKRKVKRPKPGPVAKEEPPLKKSQgptnkqlpSVAKLEMKMESIERKVSVrehgllEE 2448
Cdd:PTZ00121  1735 AKKEAEEDKKKAE-EAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKE--------AVIEEELDEEDEKRRMEV------DK 1798
                          170
                   ....*....|
gi 1958748270 2449 TTRKKKATTE 2458
Cdd:PTZ00121  1799 KIKDIFDNFA 1808
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
2307-2397 2.22e-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: 2.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2307 AQEKAKKELEETKRQEALAKEKERLQTLDEEEydaltAEQKIAFDREvRQALRERKKRELERLAREMHEKKlQQELER-- 2384
Cdd:pfam05672   53 EEERARREEEARRLEEERRREEEERQRKAEEE-----AEEREQREQE-EQERLQKQKEEAEAKAREEAERQ-RQEREKim 125
                           90
                   ....*....|....
gi 1958748270 2385 QKEEDE-LKRKvKR 2397
Cdd:pfam05672  126 QQEEQErLERK-KR 138
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
2308-2472 3.46e-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: 3.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2308 QEKAKK-----ELEETKRQEALAKEKERLQtlDEEEYDaltaEQKIAFDREVRQALRERKKR---ELERLAREMHEKKLQ 2379
Cdd:pfam15709  368 LERAEKmreelELEQQRRFEEIRLRKQRLE--EERQRQ----EEEERKQRLQLQAAQERARQqqeEFRRKLQELQRKKQQ 441
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2380 QELERQKEEdelKRKVKrpkpgpvaKEEPPLKKSQgptnKQLPSVAKlEMKMESIERKVSVREHGLLE--ETTRKKKATT 2457
Cdd:pfam15709  442 EEAERAEAE---KQRQK--------ELEMQLAEEQ----KRLMEMAE-EERLEYQRQKQEAEEKARLEaeERRQKEEEAA 505
                          170
                   ....*....|....*
gi 1958748270 2458 EYAFGFPITQEQEES 2472
Cdd:pfam15709  506 RLALEEAMKQAQEQA 520
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
2306-2489 3.52e-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: 3.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2306 KAQEKAKKELEETKRQ--EALAKEKERLQTLDE---EEYDALTAEQ--KIAFDREvRQALRERKKRELERLARE--MHEK 2376
Cdd:TIGR02794   64 KKEQERQKKLEQQAEEaeKQRAAEQARQKELEQraaAEKAAKQAEQaaKQAEEKQ-KQAEEAKAKQAAEAKAKAeaEAER 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2377 KLQQELERQKEED-------ELKRKV----KRPKPGPVAKEEpPLKKSQGPTNKQLPSVAKLEMKMESIERKvsVREHGL 2445
Cdd:TIGR02794  143 KAKEEAAKQAEEEakakaaaEAKKKAeeakKKAEAEAKAKAE-AEAKAKAEEAKAKAEAAKAKAAAEAAAKA--EAEAAA 219
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2446 LEETTRKKKATTEYAFGFP------ITQEQEESEGDFLKDSDKNLAQKFK 2489
Cdd:TIGR02794  220 AAAAEAERKADEAELGDIFglasgsNAEKQGGARGAAAGSEVDKYAAIIQ 269
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
2300-2453 3.98e-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: 3.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2300 QDYVAMKAQEKAKKELEETKRQEALAKEKErlqtldEEEydaltAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQ 2379
Cdd:TIGR02794   99 AAEKAAKQAEQAAKQAEEKQKQAEEAKAKQ------AAE-----AKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKK 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2380 QELERQKEEDELK------RKVKRPKPGpvAKEEPPLKKSQGPTNKQLPSVAKLEMKMESiERKVSVRE----HGLLEET 2449
Cdd:TIGR02794  168 AEEAKKKAEAEAKakaeaeAKAKAEEAK--AKAEAAKAKAAAEAAAKAEAEAAAAAAAEA-ERKADEAElgdiFGLASGS 244

                   ....
gi 1958748270 2450 TRKK 2453
Cdd:TIGR02794  245 NAEK 248
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
2307-2455 4.09e-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: 4.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2307 AQEKAKKELEETKRQEALAKEKERLQTLDEEEYDAL--TAEQKIAFDREVRQALRE--RKKRELERLAREMHEKKLQQEL 2382
Cdd:COG3064      1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKeeAEEERLAELEAKRQAEEEarEAKAEAEQRAAELAAEAAKKLA 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958748270 2383 ERQKEEDELKRKVKRPKPGPVAKEEPPLKKsqgptnKQLPSVAKLEmKMESIERKVsvrehglleETTRKKKA 2455
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 ...
2321-2468 6.58e-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: 6.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2321 QEALAKEKERLQTLDEEEYDALTAEQkiafDREVRQALRERKKRELERLAREMHEKKlqqelERQKEEDELKRKVKRPKP 2400
Cdd:pfam11600    8 QSQEEKEKQRLEKDKERLRRQLKLEA----EKEEKERLKEEAKAEKERAKEEARRKK-----EEEKELKEKERREKKEKD 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2401 GPVAKEEPPLKKSQgPTNKQLPSVAKLEMKMESIERKvsvrehGLLEETTRKK--KATTEYAFGFPITQE 2468
Cdd:pfam11600   79 EKEKAEKLRLKEEK-RKEKQEALEAKLEEKRKKEEEK------RLKEEEKRIKaeKAEITRFLQKPKTQQ 141
Caldesmon pfam02029
Caldesmon;
2299-2438 9.17e-07

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 55.26  E-value: 9.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2299 SQDYVAMK-AQEKAKKELEETKRqealaKEKERLQTLDEEEydaltaeqkiafdrevrqalRERKKRELERLAREMHEK- 2376
Cdd:pfam02029  262 SEEFEKLRqKQQEAELELEELKK-----KREERRKLLEEEE--------------------QRRKQEEAERKLREEEEKr 316
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958748270 2377 KLQQELERQKEEDELKRKvKRPKPGPvAKEEPPLKksqgPTNKQLPSVaKLEMKMESIERKV 2438
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 ...
2293-2407 1.03e-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: 1.03e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270  2293 IYVINMSQDYVAMKAQEKAKKELEET--KRQEALAKEKERLQTLdEEEYDA----LTAEQkiafdREVRQALRERKKREL 2366
Cdd:smart00935    1 IGVVDVQKILQESPAGKAAQKQLEKEfkKRQAELEKLEKELQKL-KEKLQKdaatLSEAA-----REKKEKELQKKVQEF 74
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1958748270  2367 ERLAREMHEK--KLQQElERQKEEDELKRKVKRpkpgpVAKEE 2407
Cdd:smart00935   75 QRKQQKLQQDlqKRQQE-ELQKILDKINKAIKE-----VAKKK 111
PTZ00121 PTZ00121
MAEBL; Provisional
2304-2455 1.08e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.53  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2304 AMKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIafdREVRQALRERKK----RELERLAREMHEKKLQ 2379
Cdd:PTZ00121  1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA---EEAKKADEAKKKaeeaKKAEEAKKKAEEAKKA 1472
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2380 QELERQKEE----DELKRKVKRPKpgpvAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKA 2455
Cdd:PTZ00121  1473 DEAKKKAEEakkaDEAKKKAEEAK----KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
2305-2388 1.18e-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: 1.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2305 MKAQEKAKKELEEtKRQEALAkEKERLqtldeEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELER 2384
Cdd:pfam20492   43 RRQAEEEAERLEQ-KRQEAEE-EKERL-----EESAEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEE 115

                   ....
gi 1958748270 2385 QKEE 2388
Cdd:pfam20492  116 AREE 119
PTZ00121 PTZ00121
MAEBL; Provisional
2304-2455 1.26e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.53  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2304 AMKAQEKAKKELEETKRQE------ALAKEKERLQTLDEEEYDALTAEQKIAFDrEVRQALRERK---------KRELER 2368
Cdd:PTZ00121  1228 AVKKAEEAKKDAEEAKKAEeernneEIRKFEEARMAHFARRQAAIKAEEARKAD-ELKKAEEKKKadeakkaeeKKKADE 1306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2369 LAREMHEKKLQQELERQKEE-----DELKRKV-KRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKL---EMKMESIERKVS 2439
Cdd:PTZ00121  1307 AKKKAEEAKKADEAKKKAEEakkkaDAAKKKAeEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKkkeEAKKKADAAKKK 1386
                          170
                   ....*....|....*.
gi 1958748270 2440 VREHGLLEETtrKKKA 2455
Cdd:PTZ00121  1387 AEEKKKADEA--KKKA 1400
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
2303-2405 1.41e-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: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2303 VAMKAQEKAKKELEETKRQealaKEKERLQTLDEEEYDaltAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQEL 2382
Cdd:pfam11600   48 EKERAKEEARRKKEEEKEL----KEKERREKKEKDEKE---KAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEE 120
                           90       100
                   ....*....|....*....|....
gi 1958748270 2383 ERQK-EEDELKRKVKRPKPGPVAK 2405
Cdd:pfam11600  121 KRIKaEKAEITRFLQKPKTQQAPK 144
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
2328-2393 1.43e-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: 1.43e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958748270 2328 KERLQTLDEEEYDALTAEQKiafdrevRQAlRERKKRE-LERLAREMHEKKLQQELERQKEEDELKR 2393
Cdd:pfam05672    1 KPSAGTTDAEEAARILAEKR-------RQA-REQREREeQERLEKEEEERLRKEELRRRAEEERARR 59
mS26_PET12 cd23703
Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...
2304-2397 2.57e-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: 2.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2304 AMKAQEKAKKELEETKRQ---EALAKEKERLQTLDEEEydaltaEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQ 2380
Cdd:cd23703     44 PLSEYQEWKRKMAELRRQnlrEGLRELEERKLKTEELR------AKRSERKQAERERALNAPEREDERLTLPTIESALLG 117
                           90       100
                   ....*....|....*....|..
gi 1958748270 2381 ELERQ-----KEEDELKRKVKR 2397
Cdd:cd23703    118 PLMRVrtdpeREERAAKRRANR 139
Caldesmon pfam02029
Caldesmon;
2313-2396 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 1958748270 2313 KELEETKRQEA---LAKEKERLQTLDEEEYDALTAEQkiafdREVRQALRE-RKKRELERLAREMHE-KKLQQELERQKE 2387
Cdd:pfam02029  236 REEEAEVFLEAeqkLEELRRRRQEKESEEFEKLRQKQ-----QEAELELEElKKKREERRKLLEEEEqRRKQEEAERKLR 310

                   ....*....
gi 1958748270 2388 EDELKRKVK 2396
Cdd:pfam02029  311 EEEEKRRMK 319
PTZ00121 PTZ00121
MAEBL; Provisional
2306-2455 3.33e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 3.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2306 KAQEKAKKElEETKRQEALAKEKERLQTLDEEEYDALTAEQKIafdREVRQALRERKKRELERLAREM----HEKKLQQE 2381
Cdd:PTZ00121  1386 KAEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKKADEAKKKA---EEKKKADEAKKKAEEAKKADEAkkkaEEAKKAEE 1461
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2382 LERQKEE----DELKRKVKRPKPGPVAKeepplKKSQGPTNK--QLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKA 2455
Cdd:PTZ00121  1462 AKKKAEEakkaDEAKKKAEEAKKADEAK-----KKAEEAKKKadEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2305-2397 3.44e-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: 3.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2305 MKAQEKAKKELEETKRQEALAKEK--ERLQTLDEEEYdALTAEQKIAFDREVRQALRERKK-RELERLAREMHEKKLQQE 2381
Cdd:pfam13868   82 IEEREQKRQEEYEEKLQEREQMDEivERIQEEDQAEA-EEKLEKQRQLREEIDEFNEEQAEwKELEKEEEREEDERILEY 160
                           90
                   ....*....|....*.
gi 1958748270 2382 LeRQKEEDELKRKVKR 2397
Cdd:pfam13868  161 L-KEKAEREEEREAER 175
PTZ00121 PTZ00121
MAEBL; Provisional
2305-2455 3.78e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 3.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2305 MKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIafdREVRQALRERKKRELERLAREM----HEKKLQQ 2380
Cdd:PTZ00121  1410 LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA---EEAKKAEEAKKKAEEAKKADEAkkkaEEAKKAD 1486
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2381 ELERQKEE-----DELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKA 2455
Cdd:PTZ00121  1487 EAKKKAEEakkkaDEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2305-2502 4.23e-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: 4.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2305 MKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEqkIAFDREVRQALRERKKRELERLAREMHE-KKLQQELE 2383
Cdd:pfam02463  254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE--EEELKSELLKLERRKVDDEEKLKESEKEkKKAEKELK 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2384 RQKEEDELKRKVKRPKPGPVAKEEppLKKSQgptnkqlpsvaklemkMESIERKVSVREHGLLEETTRKKKATTEYAfgf 2463
Cdd:pfam02463  332 KEKEEIEELEKELKELEIKREAEE--EEEEE----------------LEKLQEKLEQLEEELLAKKKLESERLSSAA--- 390
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1958748270 2464 pITQEQEESEGDFLKDSDKNLAQKFKVYDTCLKDVQNIL 2502
Cdd:pfam02463  391 -KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE 428
PTZ00121 PTZ00121
MAEBL; Provisional
2306-2453 5.85e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 5.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2306 KAQEKAKKELEETK-RQEALAK----EKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELErlaremhEKKLQQ 2380
Cdd:PTZ00121  1647 KKAEELKKAEEENKiKAAEEAKkaeeDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE-------EKKKAE 1719
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958748270 2381 ELERQKEE-----DELKRKVKRPKpgpvaKEEPPLKKSQGPTNKQLPSVAKLEMKMESIER-KVSVREHGLLEETTRKK 2453
Cdd:PTZ00121  1720 ELKKAEEEnkikaEEAKKEAEEDK-----KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKeKEAVIEEELDEEDEKRR 1793
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2303-2487 5.96e-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: 5.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2303 VAMKAQEKAKKELEETKrqEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQEL 2382
Cdd:COG1196    257 ELEAELAELEAELEELR--LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2383 ERQKEEDELKRKvkrpkpgpvAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKATTEyafg 2462
Cdd:COG1196    335 LEEELEELEEEL---------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ---- 401
                          170       180
                   ....*....|....*....|....*
gi 1958748270 2463 fpiTQEQEESEGDFLKDSDKNLAQK 2487
Cdd:COG1196    402 ---LEELEEAEEALLERLERLEEEL 423
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
2290-2400 7.00e-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: 7.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2290 REhIYVINMSQDyvaMKAQEKAKKELEETKRQEALAKEKERLQTlDEEEYDALTAEQkiafDREVRQALRERKKRELERL 2369
Cdd:pfam13863    6 RE-MFLVQLALD---AKREEIERLEELLKQREEELEKKEQELKE-DLIKFDKFLKEN----DAKRRRALKKAEEETKLKK 76
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1958748270 2370 AREMHEKKLQQELER-QKEEDELKRKVKRPKP 2400
Cdd:pfam13863   77 EKEKEIKKLTAQIEElKSEISKLEEKLEEYKP 108
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
2279-2458 7.32e-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: 7.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2279 ALICLLkAIGSREHIYVINMSQDYVAMKA----QEKAKKELEETKRQEALAKEKERlQTLDEEEYDALTAEQKIAFDREV 2354
Cdd:TIGR02794   13 LLLGLL-ILGSLYHSVKPEPGGGAEIIQAvlvdPGAVAQQANRIQQQKKPAAKKEQ-ERQKKLEQQAEEAEKQRAAEQAR 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2355 RQALRERKKRELErlAREMhEKKLQQELERQKEEDELKRKvkrPKPGPVAKEEPPL-KKSQGPTNKQLPSVAKLEMKMES 2433
Cdd:TIGR02794   91 QKELEQRAAAEKA--AKQA-EQAAKQAEEKQKQAEEAKAK---QAAEAKAKAEAEAeRKAKEEAAKQAEEEAKAKAAAEA 164
                          170       180
                   ....*....|....*....|....*
gi 1958748270 2434 ierKVSVREHGLLEETTRKKKATTE 2458
Cdd:TIGR02794  165 ---KKKAEEAKKKAEAEAKAKAEAE 186
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
2300-2394 8.18e-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: 8.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2300 QDYVAMKAQEKAKKELEET--KRQEALAKEkerLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELErlaremhEKK 2377
Cdd:pfam15346    9 EEETARRVEEAVAKRVEEEleKRKDEIEAE---VERRVEEARKIMEKQVLEELEREREAELEEERRKEEE-------ERK 78
                           90       100
                   ....*....|....*....|..
gi 1958748270 2378 LQQELER-----QKEEDELKRK 2394
Cdd:pfam15346   79 KREELERileenNRKIEEAQRK 100
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
2292-2455 1.15e-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: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2292 HIYVINMSQDYVAMKAQEKAKKEleetkrqEALAKEKERLQTLDEEEYDALtaEQKIAFDREvrqALRERKKRELERLAR 2371
Cdd:pfam09731  293 HREIDQLSKKLAELKKREEKHIE-------RALEKQKEELDKLAEELSARL--EEVRAADEA---QLRLEFEREREEIRE 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2372 EMhEKKLQQELERQKE-------------EDELKRKVKRPKPGPVAKEEpplkksqgptNKQLPSVAKLEMKMESIERKV 2438
Cdd:pfam09731  361 SY-EEKLRTELERQAEaheehlkdvlveqEIELQREFLQDIKEKVEEER----------AGRLLKLNELLANLKGLEKAT 429
                          170
                   ....*....|....*..
gi 1958748270 2439 SvrEHGLLEETTRKKKA 2455
Cdd:pfam09731  430 S--SHSEVEDENRKAQQ 444
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
2293-2407 1.29e-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: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2293 IYVINMSQDYVAMKAQEKAKKELEE--TKRQEALAKEKERLQTLdeeeYDALTAEQKIAfdrevrQALRERKKRELERLA 2370
Cdd:pfam03938    2 IGYVDMQKILEESPEGKAAQAQLEKkfKKRQAELEAKQKELQKL----YEELQKDGALL------EEEREEKEQELQKKE 71
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1958748270 2371 REMHE--KKLQQELERQKEE------DELKRKVKRpkpgpVAKEE 2407
Cdd:pfam03938   72 QELQQlqQKAQQELQKKQQEllqpiqDKINKAIKE-----VAKEK 111
Caldesmon pfam02029
Caldesmon;
2311-2477 1.69e-05

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 51.02  E-value: 1.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2311 AKKELEETKR-QEALAKEKERLQTL-DEEEYDALTAE--QKIAFDREVRQALRER-----KKRELERLAREMHEKKLQQE 2381
Cdd:pfam02029   69 AKREERRQKRlQEALERQKEFDPTIaDEKESVAERKEnnEEEENSSWEKEEKRDSrlgryKEEETEIREKEYQENKWSTE 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2382 LERQKE---EDELKRKVKRPKPGPV-AKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREhgllEETTRKKKATT 2457
Cdd:pfam02029  149 VRQAEEegeEEEDKSEEAEEVPTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGE----EEVTKLKVTTK 224
                          170       180
                   ....*....|....*....|
gi 1958748270 2458 EYAFGFPITQEQEESEGDFL 2477
Cdd:pfam02029  225 RRQGGLSQSQEREEEAEVFL 244
PRK12704 PRK12704
phosphodiesterase; Provisional
2306-2437 2.38e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 50.55  E-value: 2.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2306 KAQEKAKKELEETKRQ-EALAKEKErLQTldEEEYDALTAEqkiaFDREVRQalrerKKRELERLaremhEKKLQQELER 2384
Cdd:PRK12704    35 EAEEEAKRILEEAKKEaEAIKKEAL-LEA--KEEIHKLRNE----FEKELRE-----RRNELQKL-----EKRLLQKEEN 97
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958748270 2385 QKEEDELkrkvkrpkpgpVAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERK 2437
Cdd:PRK12704    98 LDRKLEL-----------LEKREEELEKKEKELEQKQQELEKKEEELEELIEE 139
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2304-2393 2.57e-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: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2304 AMKAQEKAKKElEETKRQEALAK---EKERLQTLDEEEYDaLTAEQKIAFDREVR---QALRERKKRELERLAREM---- 2373
Cdd:pfam13868   59 EEEEKEEERKE-ERKRYRQELEEqieEREQKRQEEYEEKL-QEREQMDEIVERIQeedQAEAEEKLEKQRQLREEIdefn 136
                           90       100
                   ....*....|....*....|
gi 1958748270 2374 HEKKLQQELERQKEEDELKR 2393
Cdd:pfam13868  137 EEQAEWKELEKEEEREEDER 156
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
2304-2396 2.72e-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: 2.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2304 AMKAQEKAKKEleETKRQEALAKEKERLQTLDEEEyDALTAEQKIAFDREVRQaLRERKKRELERLAREmHEKKLQQELE 2383
Cdd:pfam02841  198 ALTAKEKAIEA--ERAKAEAAEAEQELLREKQKEE-EQMMEAQERSYQEHVKQ-LIEKMEAEREQLLAE-QERMLEHKLQ 272
                           90
                   ....*....|....*
gi 1958748270 2384 RQKE--EDELKRKVK 2396
Cdd:pfam02841  273 EQEEllKEGFKTEAE 287
PTZ00121 PTZ00121
MAEBL; Provisional
2287-2455 3.26e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 3.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2287 IGSREHIYVINMSQDYVAMKAQEKAK----KELEETKRQEALAKEKERlQTLDEEEYdalTAEQKIAFDREVRQAlrERK 2362
Cdd:PTZ00121  1254 IRKFEEARMAHFARRQAAIKAEEARKadelKKAEEKKKADEAKKAEEK-KKADEAKK---KAEEAKKADEAKKKA--EEA 1327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2363 KRELERLAREMHEKKLQQELERQKEE---DELKRKVKRPKPGPVAKEEPplKKSQGPTNKQLPSVAKL-EMKMESIERKV 2438
Cdd:PTZ00121  1328 KKKADAAKKKAEEAKKAAEAAKAEAEaaaDEAEAAEEKAEAAEKKKEEA--KKKADAAKKKAEEKKKAdEAKKKAEEDKK 1405
                          170
                   ....*....|....*..
gi 1958748270 2439 SVREhgLLEETTRKKKA 2455
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 3.66e-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: 3.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270  227 PDELNFSTCPVKYSTQKvLLVRNIGNKDSMFHLKTRSP--YSVEPTGGILNVGESMQLEVNFEPQTVG-----NHsgKLI 299
Cdd:pfam00635    7 PDLIFFAAPGNKQGTST-LTLKNTSDKRVAFKVKTTNPkkYRVRPNYGIIKPGESVTITITRQPFDEEpgdakKD--KFV 83

                   ...
gi 1958748270  300 VIY 302
Cdd:pfam00635   84 IQY 86
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
2309-2394 4.65e-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: 4.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2309 EKAKKELEETKR-QEALAKEKER-LQTLDEEEYDAL-----TAEQKiafdREVRqALRERKKRELERLAREMHEKKLQQE 2381
Cdd:pfam15558  112 ERARQEAEQRKQcQEQRLKEKEEeLQALREQNSLQLqerleEACHK----RQLK-EREEQKKVQENNLSELLNHQARKVL 186
                           90
                   ....*....|....
gi 1958748270 2382 LERQ-KEEDELKRK 2394
Cdd:pfam15558  187 VDCQaKAEELLRRL 200
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2303-2397 4.67e-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: 4.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2303 VAMKAQEKAKKELEETKRQEALAKEKERL-----------QTLDE--EEYDALTAEQKIAFDREvRQALRERKKRELE-- 2367
Cdd:pfam13868   36 AEEKEEERRLDEMMEEERERALEEEEEKEeerkeerkryrQELEEqiEEREQKRQEEYEEKLQE-REQMDEIVERIQEed 114
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958748270 2368 -RLAREMHEKK--LQQELERQKEEDELKRKVKR 2397
Cdd:pfam13868  115 qAEAEEKLEKQrqLREEIDEFNEEQAEWKELEK 147
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2304-2397 5.01e-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: 5.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2304 AMKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERK-------KRELERLAREMHEK 2376
Cdd:pfam13868  226 EAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRrmkrlehRRELEKQIEEREEQ 305
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1958748270 2377 KL----------QQELERQKEEDELKRKVKR 2397
Cdd:pfam13868  306 RAaereeeleegERLREEEAERRERIEEERQ 336
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
2306-2399 5.28e-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: 5.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2306 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQaLRERKKRELERLARE---MHEKKLQQEL 2382
Cdd:cd16269    191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQ-LKEKMEEERENLLKEqerALESKLKEQE 269
                           90       100
                   ....*....|....*....|..
gi 1958748270 2383 ERQKEE-----DELKRKVKRPK 2399
Cdd:cd16269    270 ALLEEGfkeqaELLQEEIRSLK 291
Cgr1 pfam03879
Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA ...
2299-2399 7.03e-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: 7.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2299 SQDYVAMKAQEKAKKELEETKRQEALAKEKErLQTLDEEEydaltAEQKIAFDREvRQALRERKKReLERLAREMHEKKL 2378
Cdd:pfam03879   21 SSLVVGPKSKSWEKRQEKRLELKAIKAKEKE-LKDEKEAE-----RQRRIQAIKE-RREAKEEKER-YEELAAKMHAKKV 92
                           90       100
                   ....*....|....*....|.
gi 1958748270 2379 QQelerqkeedeLKRKVKRPK 2399
Cdd:pfam03879   93 ER----------LKRKEKRNK 103
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
2306-2457 7.36e-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: 7.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2306 KAQEKAKK-ELEETKRQEALAKEKERLQTldEEEYDALTAEQKIAfDREVRQALRERKKRELERLAREMHEKKLQQelER 2384
Cdd:COG3064     52 QAEEEAREaKAEAEQRAAELAAEAAKKLA--EAEKAAAEAEKKAA-AEKAKAAKEAEAAAAAEKAAAAAEKEKAEE--AK 126
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958748270 2385 QKEEDELKRKVKRPKPGpVAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKATT 2457
Cdd:COG3064    127 RKAEEEAKRKAEEERKA-AEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAA 198
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
2304-2408 9.75e-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: 9.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2304 AMKAQEKAKKELEETKRQEAlakEKERLQTLD-----EEEYDALTAEQKIAFDRevRQALRERKKRELERLAREMhEKKL 2378
Cdd:COG3064     20 QAEAEKRAAAEAEQKAKEEA---EEERLAELEakrqaEEEAREAKAEAEQRAAE--LAAEAAKKLAEAEKAAAEA-EKKA 93
                           90       100       110
                   ....*....|....*....|....*....|
gi 1958748270 2379 QQELERQKEEDElkRKVKRPKPGPVAKEEP 2408
Cdd:COG3064     94 AAEKAKAAKEAE--AAAAAEKAAAAAEKEK 121
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
2309-2396 9.82e-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: 47.99  E-value: 9.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2309 EKAKKELEETKRQEALAKEKERLQtlDEEEYDALtaEQKIAFDREVRQALRERKKRELERLAREmhekklqQELERQKEE 2388
Cdd:pfam13868  264 ERMLRKQAEDEEIEQEEAEKRRMK--RLEHRREL--EKQIEEREEQRAAEREEELEEGERLREE-------EAERRERIE 332

                   ....*...
gi 1958748270 2389 DELKRKVK 2396
Cdd:pfam13868  333 EERQKKLK 340
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2306-2493 9.86e-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: 9.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2306 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDaltaEQKIAFDREVRQALRERKKRELERLAREmhEKKLQQELERQ 2385
Cdd:pfam02463  201 KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLN----EERIDLLQELLRDEQEEIESSKQEIEKE--EEKLAQVLKEN 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2386 KEEdELKRKVKRPKPGPVAKEEppLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKAtTEYAFGFPI 2465
Cdd:pfam02463  275 KEE-EKEKKLQEEELKLLAKEE--EELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELE-KELKELEIK 350
                          170       180
                   ....*....|....*....|....*...
gi 1958748270 2466 TQEQEESEGDFLKDSDKNLAQKFKVYDT 2493
Cdd:pfam02463  351 REAEEEEEEELEKLQEKLEQLEEELLAK 378
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
2306-2416 1.12e-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: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2306 KAQEKAKKELEETKRQ--------------EALAKEKERLQTLDEEEYDALTAEQKIafdrEVRQALRERKKRELERLAR 2371
Cdd:NF033838   315 EAKKKAKDQKEEDRRNyptntyktleleiaESDVKVKEAELELVKEEAKEPRNEEKI----KQAKAKVESKKAEATRLEK 390
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1958748270 2372 EMHEKKLQQELERQK--EEDELKRK-VKRPKPGPVAKEEPPLKKSQGP 2416
Cdd:NF033838   391 IKTDRKKAEEEAKRKaaEEDKVKEKpAEQPQPAPAPQPEKPAPKPEKP 438
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2304-2492 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 1958748270 2304 AMKAQEKAKKELEETKRQ-----EALAKEKERLQTLdEEEYDALTAE-QKIAFDREVRQALRERKKRELERLAREMHEKK 2377
Cdd:COG4372     71 ARSELEQLEEELEELNEQlqaaqAELAQAQEELESL-QEEAEELQEElEELQKERQDLEQQRKQLEAQIAELQSEIAERE 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2378 LQ-QELERQKE--EDELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEET-TRKK 2453
Cdd:COG4372    150 EElKELEEQLEslQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKdSLEA 229
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1958748270 2454 KATTEYAFGFPITQEQEESEGDFLKDSDKNLAQKFKVYD 2492
Cdd:COG4372    230 KLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
2300-2455 1.27e-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: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2300 QDYVAMKAQEKAKKELEetKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAR-----EMH 2374
Cdd:pfam15558   26 LQQQAALAWEELRRRDQ--KRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRwreqaEDQ 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2375 EKKLQQELERQKEEDELKRK--VKRPKpgpvAKEEppLKKSQGPTNKQLpsvakLEMKMESIERKVSVREHGL---LEET 2449
Cdd:pfam15558  104 ENQRQEKLERARQEAEQRKQcqEQRLK----EKEE--ELQALREQNSLQ-----LQERLEEACHKRQLKEREEqkkVQEN 172

                   ....*.
gi 1958748270 2450 TRKKKA 2455
Cdd:pfam15558  173 NLSELL 178
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2290-2397 1.39e-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: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2290 REHIYVINMSQDYVAMKAQEKAKKELEETkrQEALAKEKERLQTLdEEEYDALTAEQkiafdREVRQALRERKKRELERL 2369
Cdd:COG4913    272 AELEYLRAALRLWFAQRRLELLEAELEEL--RAELARLEAELERL-EARLDALREEL-----DELEAQIRGNGGDRLEQL 343
                           90       100
                   ....*....|....*....|....*...
gi 1958748270 2370 AREMHEKKLQQElERQKEEDELKRKVKR 2397
Cdd:COG4913    344 EREIERLERELE-ERERRRARLEALLAA 370
YscO pfam07321
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ...
2302-2391 1.44e-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: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2302 YVAMKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDAlTAEQKIAFDREVRQALRERkKRELERLAreMHEKKLQQE 2381
Cdd:pfam07321   55 YAEIQGKLVLLKELEKVKQQVALLRENEADLEKQVAEARQ-QLEAEREALRQARQALAEA-RRAVEKFA--ELVRLVQAE 130
                           90
                   ....*....|...
gi 1958748270 2382 LERQ---KEEDEL 2391
Cdd:pfam07321  131 ELRQqerQEEQEL 143
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
2300-2531 1.51e-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: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2300 QDYVAMKAQEKAKKELEETKRQEAlakekerlqtldEEEYDALTaeQKIAFDREVRQALRERK----------KRELERL 2369
Cdd:TIGR00618  424 GQLAHAKKQQELQQRYAELCAAAI------------TCTAQCEK--LEKIHLQESAQSLKEREqqlqtkeqihLQETRKK 489
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2370 AREMHEKKLQQELERqkeedELKRKVKRPKPGPVAKEEPPLkkSQGPTNKQLPSVAKLEMKMESIerkvsvrEHGLLEET 2449
Cdd:TIGR00618  490 AVVLARLLELQEEPC-----PLCGSCIHPNPARQDIDNPGP--LTRRMQRGEQTYAQLETSEEDV-------YHQLTSER 555
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2450 TRKKkatteyafgfpITQEQEESEgdflKDSDKNLAQKFKVYDTCLKDVQNI---LMYW------DRKQGMMVPHTGPDE 2520
Cdd:TIGR00618  556 KQRA-----------SLKEQMQEI----QQSFSILTQCDNRSKEDIPNLQNItvrLQDLteklseAEDMLACEQHALLRK 620
                          250
                   ....*....|.
gi 1958748270 2521 IPHEVDDQRQA 2531
Cdd:TIGR00618  621 LQPEQDLQDVR 631
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
2309-2455 1.81e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2309 EKAKKELEETKRQeaLAKEKERLQTLdEEEYDALTAEQKiafdrEVRQALrERKKRELERLAREMheKKLQQELER-QKE 2387
Cdd:COG4372     62 EQLEEELEQARSE--LEQLEEELEEL-NEQLQAAQAELA-----QAQEEL-ESLQEEAEELQEEL--EELQKERQDlEQQ 130
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958748270 2388 EDELKRKVKRPKPGPVAKEEpplkksqgptnkQLpsvAKLEMKMESIERKVSVREHGLLEETTRKKKA 2455
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 ...
2308-2485 2.00e-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: 2.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2308 QEKAKKELEE-TKRQEALAKEKERLQtldeeeyDALTAEQKIAFDREVRQALRERKKRELERLAREMhEKKLQQELERQK 2386
Cdd:pfam01576   21 QQKAESELKElEKKHQQLCEEKNALQ-------EQLQAETELCAEAEEMRARLAARKQELEEILHEL-ESRLEEEEERSQ 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2387 EEDELKRKVKRpkpgPVAKEEPPLKKSQGPTNK-QLPSVAkLEMKMESIERKVSV---------REHGLLEEttRKKKAT 2456
Cdd:pfam01576   93 QLQNEKKKMQQ----HIQDLEEQLDEEEAARQKlQLEKVT-TEAKIKKLEEDILLledqnsklsKERKLLEE--RISEFT 165
                          170       180
                   ....*....|....*....|....*....
gi 1958748270 2457 TEYAfgfpitqEQEESEGDFLKDSDKNLA 2485
Cdd:pfam01576  166 SNLA-------EEEEKAKSLSKLKNKHEA 187
Saf4_Yju2 pfam04502
Saf4/Yju2 protein; This is a family of eukaryotic proteins that includes CCDC130 and CCDC94 ...
2304-2487 2.71e-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: 2.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2304 AMKAQEK----AKKELEETKRQEALAKEKERLQTLDeeeYDALtaeqkiafdREVRQALR-ERKKRELERLAREMHEKKL 2378
Cdd:pfam04502  130 AMKKLEKrtkdSKREMEALERLEELQELNQRQWKDD---YDAN---------LKLRREFReEKKEREEEEEDEEALKEKM 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2379 QQE-LERQKEEDELKRKVK------------RPKPGPVAKEEPPLKKSQGPTNKqlpsVAKLEMKMESIERKVSVREHGL 2445
Cdd:pfam04502  198 SLEiIKLLPEDEEDDRRAAlvefgsrplfgdSSPPAKTESPTDSLTSEISASSK----RESLKKSLGKLTRKAADPLLLG 273
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958748270 2446 LeetTRKKKATTEYAFGFPITQEQEESEGDFLKDSDKNLAQK 2487
Cdd:pfam04502  274 V---KRKKAATEEPSTPSSETSTESSKTSTPSSAQVSSSSPA 312
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
2304-2458 2.89e-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: 2.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2304 AMKAQEKAKKELEETKRQEALAKEKERLQtldeeeydaltAEQKIAFDREVRQAlRERKKRELERLAremhEKKLQQELE 2383
Cdd:COG3064     75 AAKKLAEAEKAAAEAEKKAAAEKAKAAKE-----------AEAAAAAEKAAAAA-EKEKAEEAKRKA----EEEAKRKAE 138
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958748270 2384 RQKEEDELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKATTE 2458
Cdd:COG3064    139 EERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
2309-2397 3.48e-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: 3.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2309 EKAKKELEETKRQEALAKEKERLQTL-DEEEYDALTAEqkIAFDREVRQALRERKKRELERLarEMHEKKLQQ-ELERQK 2386
Cdd:COG1579     60 EIKRLELEIEEVEARIKKYEEQLGNVrNNKEYEALQKE--IESLKRRISDLEDEILELMERI--EELEEELAElEAELAE 135
                           90
                   ....*....|.
gi 1958748270 2387 EEDELKRKVKR 2397
Cdd:COG1579    136 LEAELEEKKAE 146
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
2309-2397 4.77e-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: 4.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2309 EKAKKELEE---------TKRQEALAKEKERLQTLDEEEYDAltaeqkiafdREVRQALrERKKRELERLAREMHEKKLQ 2379
Cdd:pfam20492    5 EREKQELEErlkqyeeetKKAQEELEESEETAEELEEERRQA----------EEEAERL-EQKRQEAEEEKERLEESAEM 73
                           90       100
                   ....*....|....*....|.
gi 1958748270 2380 QELERQKEEDEL---KRKVKR 2397
Cdd:pfam20492   74 EAEEKEQLEAELaeaQEEIAR 94
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
2304-2389 5.05e-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: 5.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2304 AMKAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDA--LTAEQKiAFDREVRQALR-----ERKKREL-------ERL 2369
Cdd:pfam15236   54 ALEHQNAIKKQLEEKERQKKLEEERRRQEEQEEEERLRreREEEQK-QFEEERRKQKEkeeamTRKTQALlqamqkaQEL 132
                           90       100
                   ....*....|....*....|
gi 1958748270 2370 AREMHEKKLQQELErQKEED 2389
Cdd:pfam15236  133 AQRLKQEQRIRELA-EKGHD 151
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
2262-2416 7.47e-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: 7.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2262 GVVFDGLDTLFARNAPSALIcllkaigSRehIYVIN--MSQDYVAMKAQEKAKKELEETKrqEALAKEKERLQTL-DEEE 2338
Cdd:COG3883     99 GGSVSYLDVLLGSESFSDFL-------DR--LSALSkiADADADLLEELKADKAELEAKK--AELEAKLAELEALkAELE 167
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958748270 2339 YDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELERQKEEDELKRKVKRPKPGPVAKEEPPLKKSQGP 2416
Cdd:COG3883    168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAS 245
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
2305-2414 7.66e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.97  E-value: 7.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2305 MKAQEKAK---KELEETKR-QEALAKEKERLQtldeEEYDALTAEQKiafdREVRQALRERKKrELERLAREMHEK-KLQ 2379
Cdd:PRK00409   530 RELEQKAEeaeALLKEAEKlKEELEEKKEKLQ----EEEDKLLEEAE----KEAQQAIKEAKK-EADEIIKELRQLqKGG 600
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958748270 2380 QELERQKEEDELKRKVKRPKPgpvAKEEPPLKKSQ 2414
Cdd:PRK00409   601 YASVKAHELIEARKRLNKANE---KKEKKKKKQKE 632
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
2242-2298 8.22e-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: 8.22e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2242 PDDLLIQILAERIQLSDCFRGVVFDGldtlFARNAPSALIclLKAIGSREHI---YVINM 2298
Cdd:COG0563     60 PDEIVIGLVKERLAQPDCANGFILDG----FPRTVAQAEA--LDELLAELGIkldAVIEL 113
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
2300-2397 9.42e-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: 9.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2300 QDYVAMKAQEKAKKELEETKR-----------QEALAKEKERlQTLDEEEYDALTAEQKIAFDREVRQALRERKKREL-E 2367
Cdd:pfam15558  148 QERLEEACHKRQLKEREEQKKvqennlsellnHQARKVLVDC-QAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELrE 226
                           90       100       110
                   ....*....|....*....|....*....|
gi 1958748270 2368 RLAREmhEKKLQQELERQKEEDELKRKVKR 2397
Cdd:pfam15558  227 KAQKE--EEQFQRAKWRAEEKEEERQEHKE 254
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
2335-2460 1.13e-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: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2335 DEEEYDALTAEQKIafDREVRQALRERKK--RELERLAREMheKKLQQELERQKEE-DELKRKVKRpKPGPVAKEEPPLK 2411
Cdd:COG1579      2 MPEDLRALLDLQEL--DSELDRLEHRLKElpAELAELEDEL--AALEARLEAAKTElEDLEKEIKR-LELEIEEVEARIK 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958748270 2412 KSQgptnKQLPSVAK------LEMKMESIERKVSVREHGLLEETTRKKKATTEYA 2460
Cdd:COG1579     77 KYE----EQLGNVRNnkeyeaLQKEIESLKRRISDLEDEILELMERIEELEEELA 127
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
2312-2575 1.36e-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: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2312 KKELEETKRQEALAK-EKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKR---ELERLAREMhekklQQELERQKE 2387
Cdd:pfam17380  281 QKAVSERQQQEKFEKmEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyaEQERMAMER-----ERELERIRQ 355
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2388 EDElKRKVKRPKPGPVAKEeppLKKSQGPTNKQLPSVAKLEMKMESIErkvSVREHGLLEETtRKKKATTEYAFGFPITQ 2467
Cdd:pfam17380  356 EER-KRELERIRQEEIAME---ISRMRELERLQMERQQKNERVRQELE---AARKVKILEEE-RQRKIQQQKVEMEQIRA 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2468 EQEESEGDFLKDSDKNLAQKfkvydtclkdvqnilMYWDRKQGMmvphtgpdEIPHEVDDQRQAPSGGGGRKGRKDRERe 2547
Cdd:pfam17380  428 EQEEARQREVRRLEEERARE---------------MERVRLEEQ--------ERQQQVERLRQQEEERKRKKLELEKEK- 483
                          250       260
                   ....*....|....*....|....*...
gi 1958748270 2548 rleKERAEKERLEREKAERERLEKLRAM 2575
Cdd:pfam17380  484 ---RDRKRAEEQRRKILEKELEERKQAM 508
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
2310-2412 1.43e-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: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2310 KAKKELEetkrQEALAKEKERLQTLDEEeydaltaEQKIAFDREVRQALRERKKRELERLAREMHEK--KLQQELERQKE 2387
Cdd:pfam00992   11 KAAEELE----FEQEKKEEEKLRYLAER-------IPPLRLRGLSAEQLQELCEELHERIDKLEEERydIEEKVAKKDKE 79
                           90       100
                   ....*....|....*....|....*..
gi 1958748270 2388 EDELKRKV--KRPKPGPvakeePPLKK 2412
Cdd:pfam00992   80 INDLKKKVndLRGKFKK-----PLLKK 101
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2306-2397 1.49e-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: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2306 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELERQ 2385
Cdd:COG1196    666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
                           90       100
                   ....*....|....*....|....*.
gi 1958748270 2386 KE--------------EDELKRKVKR 2397
Cdd:COG1196    746 ELleeealeelpeppdLEELERELER 771
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
2305-2396 1.78e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.41  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2305 MKAQEKAK-KELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELE 2383
Cdd:PRK09510   103 LKQLEKERlAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE 182
                           90
                   ....*....|....
gi 1958748270 2384 RQKE-EDELKRKVK 2396
Cdd:PRK09510   183 AKKKaEAEAAAKAA 196
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2303-2397 1.95e-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: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2303 VAMKAQEKaKKELEETKRQEALAKEKERLQTLD--EEEYDALTAE-QKIAFDREVRQALRERKKRELERLAREMHEKKlQ 2379
Cdd:COG1196    211 KAERYREL-KEELKELEAELLLLKLRELEAELEelEAELEELEAElEELEAELAELEAELEELRLELEELELELEEAQ-A 288
                           90
                   ....*....|....*...
gi 1958748270 2380 QELERQKEEDELKRKVKR 2397
Cdd:COG1196    289 EEYELLAELARLEQDIAR 306
adk PRK00279
adenylate kinase; Reviewed
2242-2298 2.25e-03

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 42.83  E-value: 2.25e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958748270 2242 PDDLLIQILAERIQLSDCFRGVVFDGldtlFARNAP--SALICLLKAIGsREHIYVINM 2298
Cdd:PRK00279    60 PDEIVIGLVKERLAQPDCKNGFLLDG----FPRTIPqaEALDEMLKELG-IKLDAVIEI 113
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2304-2393 2.31e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2304 AMKAQEKAKKELEETKRQEALAKEKERLQTLDE-----EEYDALTAEQkiafdREVRQALrERKKRELERLAREMheKKL 2378
Cdd:COG4717    161 LEEELEELEAELAELQEELEELLEQLSLATEEElqdlaEELEELQQRL-----AELEEEL-EEAQEELEELEEEL--EQL 232
                           90
                   ....*....|....*
gi 1958748270 2379 QQELERQKEEDELKR 2393
Cdd:COG4717    233 ENELEAAALEERLKE 247
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2308-2397 2.39e-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: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2308 QEKAKKELEETKRQ-EALAKEKERLQTLDEEEYDALTAEQKiafDREVRQALRERKKRELERLAREM-HEKKLQQELERQ 2385
Cdd:COG1196    241 LEELEAELEELEAElEELEAELAELEAELEELRLELEELEL---ELEEAQAEEYELLAELARLEQDIaRLEERRRELEER 317
                           90
                   ....*....|..
gi 1958748270 2386 KEEDELKRKVKR 2397
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 ...
2283-2487 2.96e-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: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2283 LLKAIG-SREHIYVINMSQDY--VAMKAQEKAKKELEETKRQEALAKEKERLQTLDEEeydALTAEQKIAFDREVRQALR 2359
Cdd:pfam02463  124 LLESQGiSPEAYNFLVQGGKIeiIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEE---TENLAELIIDLEELKLQEL 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2360 ERKKRELERLAREMHEKKLQQELERQKEEDELKRKVKRpkpgpvakeeppLKKSQGPTNKQLPSVAKLEMKMESIERKvS 2439
Cdd:pfam02463  201 KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER------------IDLLQELLRDEQEEIESSKQEIEKEEEK-L 267
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1958748270 2440 VREHGLLEETTRKKKATTEYAfGFPITQEQEESEGDFLKDSDKNLAQK 2487
Cdd:pfam02463  268 AQVLKENKEEEKEKKLQEEEL-KLLAKEEEELKSELLKLERRKVDDEE 314
FliJ COG2882
Flagellar biosynthesis chaperone FliJ [Cell motility];
2306-2391 4.18e-03

Flagellar biosynthesis chaperone FliJ [Cell motility];


Pssm-ID: 442129 [Multi-domain]  Cd Length: 142  Bit Score: 40.66  E-value: 4.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2306 KAQEKAKKELeeTKRQEALAKEKERLQTLDE--EEY---------------------------DALTAEQKIAFDR---- 2352
Cdd:COG2882     16 KEEDEAAREL--GQAQQALEQAEEQLEQLEQyrEEYeqrlqqklqqglsaaqlrnyqqfiarlDEAIEQQQQQVAQaeqq 93
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1958748270 2353 --EVRQALRERKKRE--LERLaREMHEKKLQQELER--QKEEDEL 2391
Cdd:COG2882     94 veQARQAWLEARQERkaLEKL-KERRREEERQEENRreQKELDEL 137
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
2304-2388 4.49e-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: 4.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2304 AMKAQEKAKKELEETKRQeaLAKEKERLQTLDEEEYDAL----TAEQKIAFDREVRQALRER---KKRELERLAREmhEK 2376
Cdd:COG4942     18 QADAAAEAEAELEQLQQE--IAELEKELAALKKEEKALLkqlaALERRIAALARRIRALEQElaaLEAELAELEKE--IA 93
                           90
                   ....*....|..
gi 1958748270 2377 KLQQELERQKEE 2388
Cdd:COG4942     94 ELRAELEAQKEE 105
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2309-2453 4.92e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 4.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2309 EKAKKELEE-TKRQEALAKEKERLQTLDEEEYDALTAEQKI----AFDREVRQALRER------KKRELERLAREmhEKK 2377
Cdd:PRK03918   272 KKEIEELEEkVKELKELKEKAEEYIKLSEFYEEYLDELREIekrlSRLEEEINGIEERikeleeKEERLEELKKK--LKE 349
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958748270 2378 LQQELERQKEEDELKRKVKRPKpgpvaKEEPPLKKSQGPTNKQlpsvaKLEMKMESIE-RKVSVREHglLEETTRKK 2453
Cdd:PRK03918   350 LEKRLEELEERHELYEEAKAKK-----EELERLKKRLTGLTPE-----KLEKELEELEkAKEEIEEE--ISKITARI 414
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2306-2397 5.28e-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: 5.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2306 KAQEKAKKELEE-TKRQEALakekERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKrELERLAREmhEKKLQQELER 2384
Cdd:COG4913    631 ERLEALEAELDAlQERREAL----QRLAEYSWDEIDVASAEREIAELEAELERLDASSD-DLAALEEQ--LEELEAELEE 703
                           90
                   ....*....|....
gi 1958748270 2385 QKEE-DELKRKVKR 2397
Cdd:COG4913    704 LEEElDELKGEIGR 717
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2305-2415 6.90e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 6.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2305 MKAQEKAKKELEE-TKRQEALAKEKERLQTlDEEEYDalTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELE 2383
Cdd:PRK03918   330 IKELEEKEERLEElKKKLKELEKRLEELEE-RHELYE--EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEE 406
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1958748270 2384 RQKEED---ELKRKVKRPKPgpvAKEEppLKKSQG 2415
Cdd:PRK03918   407 ISKITArigELKKEIKELKK---AIEE--LKKAKG 436
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
2306-2394 7.46e-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: 7.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2306 KAQEKAKKELEETKRQEALAKEKERLQTLDEEEYDALTAEQKIAFDREVRQALRERKKRELERLAREMHEKKLQQELERQ 2385
Cdd:COG1196    366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445

                   ....*....
gi 1958748270 2386 KEEDELKRK 2394
Cdd:COG1196    446 EAAEEEAEL 454
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
2345-2470 8.82e-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: 8.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2345 EQKI-AFDREVRQALRERKKR---------ELERLAREMHEKKLQqeLERQKEEDELKRKVKrpkpgpvAKEE--PPLKK 2412
Cdd:pfam06391   67 EKKIeQYEKENKDLILKNKMKlsqeeeeleELLELEKREKEERRK--EEKQEEEEEKEKKEK-------AKQEliDELMT 137
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958748270 2413 SQGPTNKQLPSVAKLEMKMESIERKVSVREHGLLEETTRKKKATTEYAFGFPITQEQE 2470
Cdd:pfam06391  138 SNKDAEEIIAQHKKTAKKRKSERRRKLEELNRVLEQKPTQFSTGIKFGQLPVPKIEEG 195
BBC smart00502
B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains
2309-2394 8.84e-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: 8.84e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270  2309 EKAKKELEETKRqeALAKEKERLQTLdEEEYDALTAEQKIAFDrEVRQALRERKKRELERL--AREMHEKKLQQELER-Q 2385
Cdd:smart00502   10 TKLRKKAAELED--ALKQLISIIQEV-EENAADVEAQIKAAFD-ELRNALNKRKKQLLEDLeeQKENKLKVLEQQLESlT 85

                    ....*....
gi 1958748270  2386 KEEDELKRK 2394
Cdd:smart00502   86 QKQEKLSHA 94
PTZ00121 PTZ00121
MAEBL; Provisional
2304-2609 9.95e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 9.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2304 AMKAQEKAK----KELEETKRQEAL--AKEKERLQTLDEEEyDALTAEQKiafdREVRQALR--ERKKRELER--LAREM 2373
Cdd:PTZ00121  1515 AKKAEEAKKadeaKKAEEAKKADEAkkAEEKKKADELKKAE-ELKKAEEK----KKAEEAKKaeEDKNMALRKaeEAKKA 1589
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2374 HEK------KLQQELERQKEEDELKRKVKRPKPGPVAKEEPPLKKSQGPTNKQLPSVAKLE-MKMESIERKVSVREHGLL 2446
Cdd:PTZ00121  1590 EEArieevmKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEeLKKAEEENKIKAAEEAKK 1669
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2447 EETTRKKKATTEYAfgfpitQEQEESEGDFLKdsdKNLAQKFKVYDTCLKDVQNILMYWDRKQGMMVPHTGPDEIPHEVD 2526
Cdd:PTZ00121  1670 AEEDKKKAEEAKKA------EEDEKKAAEALK---KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958748270 2527 -DQRQAPSGGGGRKGRKDRERErlekeraekERLEREKAERERLEKLRAMEERSDGEGEGEEEHEGK--KDLGVPFINIQ 2603
Cdd:PTZ00121  1741 eDKKKAEEAKKDEEEKKKIAHL---------KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKkiKDIFDNFANII 1811

                   ....*.
gi 1958748270 2604 TPDFEG 2609
Cdd:PTZ00121  1812 EGGKEG 1817
 
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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