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Conserved domains on  [gi|46048213|ref|NP_033770.2|]
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angiopoietin-1 isoform 1 precursor [Mus musculus]

Protein Classification

RILP-like and FReD domain-containing protein (domain architecture ID 11040816)

RILP-like and FReD domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
281-496 2.98e-125

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


:

Pssm-ID: 238040  Cd Length: 215  Bit Score: 366.95  E-value: 2.98e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213 281 KPFRDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNE 360
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPPGSNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213 361 FIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSlILHGADFSTKDADNDNCMCKCA 440
Cdd:cd00087  81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTAGDALS-YHNGMKFSTFDRDNDGASGNCA 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46048213 441 LMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPL 496
Cdd:cd00087 160 ESYSGGWWYNSCHASNLNGRYYSGGHRNEYDNGINWATWKGSTYSLKFTEMKIRPK 215
RILP-like super family cl23720
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
133-238 6.66e-03

Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.


The actual alignment was detected with superfamily member pfam11559:

Pssm-ID: 304877  Cd Length: 151  Bit Score: 36.15  E-value: 6.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   133 SLLSQTAEQTRKLTDVETQVlnQTSRLEIQLLENSLStyKLEKQLLQQTNEIlkiheknSLLEHKILEMEGKHKEELDTL 212
Cdd:pfam11559  42 ELLQQRDRDLEFRESLNETI--RTLEADIERLQNKIE--RLKTQLEDLEREL-------ALLQAKERQLEKKLKTLEQKL 110
                          90       100
                  ....*....|....*....|....*.
gi 46048213   213 KEEKENLQglvsRQTFIIQELEKQLS 238
Cdd:pfam11559 111 KNEKEELQ----RLKNAIQQRKTQYA 132
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
281-496 2.98e-125

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


Pssm-ID: 238040  Cd Length: 215  Bit Score: 366.95  E-value: 2.98e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213 281 KPFRDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNE 360
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPPGSNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213 361 FIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSlILHGADFSTKDADNDNCMCKCA 440
Cdd:cd00087  81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTAGDALS-YHNGMKFSTFDRDNDGASGNCA 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46048213 441 LMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPL 496
Cdd:cd00087 160 ESYSGGWWYNSCHASNLNGRYYSGGHRNEYDNGINWATWKGSTYSLKFTEMKIRPK 215
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
283-496 3.08e-123

Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and gamma chains, and a variety of fibrinogen-related proteins, including tenascin and Drosophila scabrous.


Pssm-ID: 214548  Cd Length: 212  Bit Score: 361.98  E-value: 3.08e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    283 FRDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFI 362
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGSSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    363 FAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALM 442
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGYSGTAGDASLTYHNGMQFSTYDRDNDKYSGNCAEE 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 46048213    443 LTGGWWFDACGPSNLNGMFYtagQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPL 496
Cdd:smart00186 162 YGGGWWYNNCHAANLNGRYY---PNNNYDNGINWATWKGSWYSLKFTEMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
284-496 1.27e-74

Fibrinogen beta and gamma chains, C-terminal globular domain;


Pssm-ID: 278572  Cd Length: 221  Bit Score: 237.04  E-value: 1.27e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   284 RDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPS-GEYWLGNEFI 362
Cdd:pfam00147   3 RDCSDVYNKGAKTSGLYTIRPDGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLSpGEFWLGNDKI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   363 FAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQ-----SSLILH-GADFSTKDADNDNCM 436
Cdd:pfam00147  83 HLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYIGDAGDAldtagRSMTYHnGMQFSTWDRDNDSPD 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   437 CKCALMLTGGWWFDACGPSNLNGMFYTaGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPL 496
Cdd:pfam00147 163 GNCALSYGGGWWYNNCHAANLNGVYYY-GGTYSKQNGIIWATWKGRWYSMKKAEMKIRPL 221
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
133-238 6.66e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 288418  Cd Length: 151  Bit Score: 36.15  E-value: 6.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   133 SLLSQTAEQTRKLTDVETQVlnQTSRLEIQLLENSLStyKLEKQLLQQTNEIlkiheknSLLEHKILEMEGKHKEELDTL 212
Cdd:pfam11559  42 ELLQQRDRDLEFRESLNETI--RTLEADIERLQNKIE--RLKTQLEDLEREL-------ALLQAKERQLEKKLKTLEQKL 110
                          90       100
                  ....*....|....*....|....*.
gi 46048213   213 KEEKENLQglvsRQTFIIQELEKQLS 238
Cdd:pfam11559 111 KNEKEELQ----RLKNAIQQRKTQYA 132
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
81-256 4.90e-06

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 47.83  E-value: 4.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213  81 QKLQHLEHVMENYTQWLQKLENYivENMKSEMAQIQQNAVQNHTatmleigtSLLSQTAEQTRKLTDVETQVLNQTSRLE 160
Cdd:COG0419 239 ERLAELEEEKERLEELKARLLEI--ESLELEALKIREEELRELE--------RLLEELEEKIERLEELEREIEELEEELE 308
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213 161 IQL-LENSLStyKLEKQLLQQTNEILKIHEKNSLLEHKILEMEgKHKEELDTLKEEKENLQGLvsrqtfIIQELEKQLSR 239
Cdd:COG0419 309 GLRaLLEELE--ELLEKLKSLEERLEKLEEKLEKLESELEELA-EEKNELAKLLEERLKELEE------RLEELEKELEK 379
                       170
                ....*....|....*..
gi 46048213 240 ATNNNSILQKQQLELMD 256
Cdd:COG0419 380 ALERLKQLEEAIQELKE 396
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
105-258 2.10e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.78  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   105 VENMKSEMAQIQQNAVQNhtatmleIGTSLLSQTAEQTRKLTDVETQVLNQTSRleIQLLENSLSTYKLEKQLLQQTNEI 184
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQD-------WNKELKSELKNQEKKLEEIQNQISQNNKI--ISQLNEQISQLKKELTNSESENSE 360
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46048213   185 LK--IHEKNSLLEHKILEMEGKhKEELDTLKEEKENLQGLVSRQTFIIQELEKQLSRATNNNSILQKQQLELMDTV 258
Cdd:TIGR04523 361 KQreLEEKQNEIEKLKKENQSY-KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
90-258 6.87e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 290562 [Multi-domain]  Cd Length: 200  Bit Score: 42.59  E-value: 6.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    90 MENYTQWLQKLENY---IVEN-------MKSEMAQIQQNAVQNhtatmleigTSLLSQTAEQTRKLTdvetQVLNQtSRL 159
Cdd:pfam13851   3 MKNHEKAFNEIKNYyndITLNnleliksLKEEIEEMKKKEERN---------EKLMSEIQQENKRLT----EPLKK-AEE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   160 EIQLLENSLSTYKLEKQLLQQTNEILKIHE---KNSLLEHKILEMegkhkeELDTLKEEKENLQglvSRQTFIIQELeKQ 236
Cdd:pfam13851  69 EVEELRKQLKNYEKDKQSLKNLKARLKVLEkelKDLKWEHEVLEQ------RFEKVERERDELY---KKFEDAIQDV-QQ 138
                         170       180
                  ....*....|....*....|..
gi 46048213   237 lsRATNNNSILQKQQLELMDTV 258
Cdd:pfam13851 139 --KTGLKNLLLEKKLQALQETL 158
PRK10935 PRK10935
nitrate/nitrite sensor protein NarQ; Provisional
122-255 1.62e-03

nitrate/nitrite sensor protein NarQ; Provisional


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 39.45  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213  122 NHTATmlEIGT---SLLSQTAEQTRKLTDV--ETQVLNQTSRLeiqllensLSTYKLEKQLLQQTNEILKIHEKNSLLEH 196
Cdd:PRK10935 216 NQMSS--ELHKlyrSLEASVEEKTRKLTQAnrSLEVLYQCSQA--------LNASQIDVHCFRHILQIVRDHEGLDYLEL 285
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46048213  197 KILE------MEGKHKEELD----TLKEEKENL------QGLVSRQTFIIQELEKQLSRA-TNNNSILQKQQLELM 255
Cdd:PRK10935 286 EVGEnehwriSEGQPNPELPwqilPLTMEDTVLgylhwqASLPCPDEPLMNNVAQMLGRGlYFNQAQKQQQQLLLM 361
 
Name Accession Description Interval E-value
FReD cd00087
Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is ...
281-496 2.98e-125

Fibrinogen-related domains (FReDs); C terminal globular domain of fibrinogen. Fibrinogen is involved in blood clotting, being activated by thrombin to assemble into fibrin clots. The N-termini of 2 times 3 chains come together to form a globular arrangement called the disulfide knot. The C termini of fibrinogen chains end in globular domains, which are not completely equivalent. C terminal globular domains of the gamma chains (C-gamma) dimerize and bind to the GPR motif of the N-terminal domain of the alpha chain, while the GHR motif of N-terminal domain of the beta chain binds to the C terminal globular domains of another beta chain (C-beta), which leads to lattice formation.


Pssm-ID: 238040  Cd Length: 215  Bit Score: 366.95  E-value: 2.98e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213 281 KPFRDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNE 360
Cdd:cd00087   1 PLPRDCSEVLQRGGRTSGVYTIQPPGSNEPFQVYCDMDTDGGGWTVIQRRGDGSVDFYRSWKEYKDGFGNLDGEFWLGLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213 361 FIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSlILHGADFSTKDADNDNCMCKCA 440
Cdd:cd00087  81 KIHLLTSQGPYELRIDLEDWEGNTAYAEYDSFKVGSESEGYRLTLGGYSGTAGDALS-YHNGMKFSTFDRDNDGASGNCA 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46048213 441 LMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPL 496
Cdd:cd00087 160 ESYSGGWWYNSCHASNLNGRYYSGGHRNEYDNGINWATWKGSTYSLKFTEMKIRPK 215
FBG smart00186
Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and ...
283-496 3.08e-123

Fibrinogen-related domains (FReDs); Domain present at the C-termini of fibrinogen beta and gamma chains, and a variety of fibrinogen-related proteins, including tenascin and Drosophila scabrous.


Pssm-ID: 214548  Cd Length: 212  Bit Score: 361.98  E-value: 3.08e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    283 FRDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFI 362
Cdd:smart00186   2 PRDCSDVLQNGGKTSGLYTIYPDGSSRPLKVYCDMETDGGGWTVIQRRMDGSVDFYRDWKDYKEGFGNLAGEFWLGNENI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    363 FAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALM 442
Cdd:smart00186  82 HLLTSQGKYELRIDLEDWEGNTAYALYDSFKVADEADGYRLHIGGYSGTAGDASLTYHNGMQFSTYDRDNDKYSGNCAEE 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 46048213    443 LTGGWWFDACGPSNLNGMFYtagQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPL 496
Cdd:smart00186 162 YGGGWWYNNCHAANLNGRYY---PNNNYDNGINWATWKGSWYSLKFTEMKIRPL 212
Fibrinogen_C pfam00147
Fibrinogen beta and gamma chains, C-terminal globular domain;
284-496 1.27e-74

Fibrinogen beta and gamma chains, C-terminal globular domain;


Pssm-ID: 278572  Cd Length: 221  Bit Score: 237.04  E-value: 1.27e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   284 RDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPS-GEYWLGNEFI 362
Cdd:pfam00147   3 RDCSDVYNKGAKTSGLYTIRPDGATKPFEVYCDMETDGGGWTVFQRRLDGSTNFKRNWKDYKAGFGNLSpGEFWLGNDKI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   363 FAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQ-----SSLILH-GADFSTKDADNDNCM 436
Cdd:pfam00147  83 HLLTKQGPYVLRIDLEDWNGETVFALYDSFKVTNENDKYRLHVENYIGDAGDAldtagRSMTYHnGMQFSTWDRDNDSPD 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   437 CKCALMLTGGWWFDACGPSNLNGMFYTaGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPL 496
Cdd:pfam00147 163 GNCALSYGGGWWYNNCHAANLNGVYYY-GGTYSKQNGIIWATWKGRWYSMKKAEMKIRPL 221
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
133-238 6.66e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 288418  Cd Length: 151  Bit Score: 36.15  E-value: 6.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   133 SLLSQTAEQTRKLTDVETQVlnQTSRLEIQLLENSLStyKLEKQLLQQTNEIlkiheknSLLEHKILEMEGKHKEELDTL 212
Cdd:pfam11559  42 ELLQQRDRDLEFRESLNETI--RTLEADIERLQNKIE--RLKTQLEDLEREL-------ALLQAKERQLEKKLKTLEQKL 110
                          90       100
                  ....*....|....*....|....*.
gi 46048213   213 KEEKENLQglvsRQTFIIQELEKQLS 238
Cdd:pfam11559 111 KNEKEELQ----RLKNAIQQRKTQYA 132
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
161-273 7.21e-03

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 286787  Cd Length: 154  Bit Score: 36.04  E-value: 7.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   161 IQLLENSLSTYKlEKQLLQQTNEILKiHEKNSLLEHKILEMEG--KHKEEL----DTLKEEKENLQGLVSRQTFIIQELE 234
Cdd:pfam09744  31 VRVLELLDSLAK-RNQEHEAELEELR-EDNEQLQTQYEREKELrkKAEEELleleDQWEEERKELQSKVEQLEEENRQLE 108
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 46048213   235 KQLSRATNNNSILQKQQLELMDTVHNLISLCTKegVLLK 273
Cdd:pfam09744 109 LKAKNAADQISRLEEKEAELKREYSSLHERENE--LLRK 145
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
81-256 4.90e-06

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 47.83  E-value: 4.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213  81 QKLQHLEHVMENYTQWLQKLENYivENMKSEMAQIQQNAVQNHTatmleigtSLLSQTAEQTRKLTDVETQVLNQTSRLE 160
Cdd:COG0419 239 ERLAELEEEKERLEELKARLLEI--ESLELEALKIREEELRELE--------RLLEELEEKIERLEELEREIEELEEELE 308
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213 161 IQL-LENSLStyKLEKQLLQQTNEILKIHEKNSLLEHKILEMEgKHKEELDTLKEEKENLQGLvsrqtfIIQELEKQLSR 239
Cdd:COG0419 309 GLRaLLEELE--ELLEKLKSLEERLEKLEEKLEKLESELEELA-EEKNELAKLLEERLKELEE------RLEELEKELEK 379
                       170
                ....*....|....*..
gi 46048213 240 ATNNNSILQKQQLELMD 256
Cdd:COG0419 380 ALERLKQLEEAIQELKE 396
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
81-280 1.42e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 46.25  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   81 QKLQHLEHVMENYTQWLQKLENYI--VENMKSEMAQIQQNAVQNHTAtmLEIGTSLLSQTAEQTRKLTDVETQVLNQTSR 158
Cdd:COG1196  734 QLQSRLEELEEELEELEEELEELQerLEELEEELESLEEALAKLKEE--IEELEEKRQALQEELEELEEELEEAERRLDA 811
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213  159 LEIQLLENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGK---HKEELDTLKEEKENLQGLVSRQTFIIQELEK 235
Cdd:COG1196  812 LERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKEleeLKEELEELEAEKEELEDELKELEEEKEELEE 891
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 46048213  236 QLSRATNNNSILQKQQLELMDTVHNLISLCTKEGVLLKggKREEE 280
Cdd:COG1196  892 ELRELESELAELKEEIEKLRERLEELEAKLERLEVELP--ELEEE 934
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
105-258 2.10e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.78  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   105 VENMKSEMAQIQQNAVQNhtatmleIGTSLLSQTAEQTRKLTDVETQVLNQTSRleIQLLENSLSTYKLEKQLLQQTNEI 184
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQD-------WNKELKSELKNQEKKLEEIQNQISQNNKI--ISQLNEQISQLKKELTNSESENSE 360
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46048213   185 LK--IHEKNSLLEHKILEMEGKhKEELDTLKEEKENLQGLVSRQTFIIQELEKQLSRATNNNSILQKQQLELMDTV 258
Cdd:TIGR04523 361 KQreLEEKQNEIEKLKKENQSY-KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
90-258 6.87e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 290562 [Multi-domain]  Cd Length: 200  Bit Score: 42.59  E-value: 6.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    90 MENYTQWLQKLENY---IVEN-------MKSEMAQIQQNAVQNhtatmleigTSLLSQTAEQTRKLTdvetQVLNQtSRL 159
Cdd:pfam13851   3 MKNHEKAFNEIKNYyndITLNnleliksLKEEIEEMKKKEERN---------EKLMSEIQQENKRLT----EPLKK-AEE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   160 EIQLLENSLSTYKLEKQLLQQTNEILKIHE---KNSLLEHKILEMegkhkeELDTLKEEKENLQglvSRQTFIIQELeKQ 236
Cdd:pfam13851  69 EVEELRKQLKNYEKDKQSLKNLKARLKVLEkelKDLKWEHEVLEQ------RFEKVERERDELY---KKFEDAIQDV-QQ 138
                         170       180
                  ....*....|....*....|..
gi 46048213   237 lsRATNNNSILQKQQLELMDTV 258
Cdd:pfam13851 139 --KTGLKNLLLEKKLQALQETL 158
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
77-261 7.06e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 44.32  E-value: 7.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   77 DFSSQKLQHLEHVMENYTQWLQKLENYIvENMKSEMAQIQQNaVQNHTATMLEIGTSLlSQTAEQTRKLTDVETQVLNQT 156
Cdd:COG1196  663 LAQKRELKELEEELAELEAQLEKLEEEL-KSLKNELRSLEDL-LEELRRQLEELERQL-EELKRELAALEEELEQLQSRL 739
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213  157 SRLEIQLLENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGK----------HKEELDTLKEEKENLQGLVSRQ 226
Cdd:COG1196  740 EELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKrqalqeeleeLEEELEEAERRLDALERELESL 819
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 46048213  227 TFIIQELEKQLSRATNNNSILQKQQLELMDTVHNL 261
Cdd:COG1196  820 EQRRERLEQEIEELEEEIEELEEKLDELEEELEEL 854
DUF724 pfam05266
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ...
172-217 1.28e-04

Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.


Pssm-ID: 283038 [Multi-domain]  Cd Length: 187  Bit Score: 41.46  E-value: 1.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 46048213   172 KLEKQLLQQTNEILKIHEKNSLLEHKILEMEgkhkEELDTLKEEKE 217
Cdd:pfam05266 113 KLEKKIAEKESEKRKLEEEIDELDRKILELE----RQLALLREKKE 154
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
176-244 1.88e-04

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 41.65  E-value: 1.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46048213   176 QLLQQTNEILKIHEKNSllehkilEMEGKHKEELDTLKEEKENLQGLVSRQTFIIQELEKQLSRATNNN 244
Cdd:pfam17078  21 QLTVQSQNLLSKLEIAQ-------QKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSY 82
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
59-256 2.69e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 2.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213     59 TEQYNTNALQRDAPHvEPDFSSQKLQHLEHVMENYTQWLQKLENYIVE-NMKSEMAQIQQNAVQNHTATMLEIGTSLLSQ 137
Cdd:TIGR02168  288 KELYALANEISRLEQ-QKQILRERLANLERQLEELEAQLEELESKLDElAEELAELEEKLEELKEELESLEAELEELEAE 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    138 TAEQTRKLTDVETQVLNQTSRL------------EIQLLENSLStyKLEKQLLQQTNEILKIHEKNSLLEHKILEME-GK 204
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRSKVaqlelqiaslnnEIERLEARLE--RLEDRRERLQQEIEELLKKLEEAELKELQAElEE 444
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 46048213    205 HKEELDTLKEEKENLQGLVSRQ-------TFIIQELEKQLSRATNNNSILQKQQLELMD 256
Cdd:TIGR02168  445 LEEELEELQEELERLEEALEELreeleeaEQALDAAERELAQLQARLDSLERLQENLEG 503
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
106-261 2.76e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 285171 [Multi-domain]  Cd Length: 545  Bit Score: 42.13  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   106 ENMKSEMAQIQQN-AVQNHTATMLeiGTSLLSQTAEQTRKLTDVEtQVLNQTSRLEIQLLENSL------STYKLEKQLL 178
Cdd:pfam07888 290 EALLEELRSLQERlNASERKVEGL--GEELSSMAAQRDRTQAELH-QARLQAAQLTLQLADASLalregrARWAQERETL 366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   179 QQTNEilKIHEKNSLLEHKILEMEGKHKEE------LDT-LKEEKENLQGLVSRQTFIIQELEKQLSRATNNNSILQKQQ 251
Cdd:pfam07888 367 QQSAE--ADKDRILKLSAELQRLEERLQEErmerekLEVeLGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK 444
                         170
                  ....*....|
gi 46048213   252 LELMDTVHNL 261
Cdd:pfam07888 445 QELLEYIRQL 454
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
82-250 3.09e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.93  E-value: 3.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    82 KLQHLEHVMENYTQWLQKLENYIVEnMKSEMAQIQQNAVQNHTAtmLEIGTSLLSQTAEQTRKLTDVETQVLNQTSRLEI 161
Cdd:TIGR04523 198 KLELLLSNLKKKIQKNKSLESQISE-LKKQNNQLKDNIEKKQQE--INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   162 QLLENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKILemegkhKEELDTLKEEKENLQGLVSRQTFIIQEL-------E 234
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKEL------KSELKNQEKKLEEIQNQISQNNKIISQLneqisqlK 348
                         170
                  ....*....|....*.
gi 46048213   235 KQLSRATNNNSILQKQ 250
Cdd:TIGR04523 349 KELTNSESENSEKQRE 364
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
83-258 3.53e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 3.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213     83 LQHLEHVMENYTQWLQKLE---NYIVENMKSEMAQI------QQNAVQnhtATMLEIGT---SLLSQTAEQTRKLTDVET 150
Cdd:TIGR02169  246 LASLEEELEKLTEEISELEkrlEEIEQLLEELNKKIkdlgeeEQLRVK---EKIGELEAeiaSLERSIAEKERELEDAEE 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    151 QVLNQTSRL-----EIQLLENSLSTYKLEKQLLqqTNEILKIHEKNSLLEHKILEMEGKH----------KEELDTLKEE 215
Cdd:TIGR02169  323 RLAKLEAEIdkllaEIEELEREIEEERKRRDKL--TEEYAELKEELEDLRAELEEVDKEFaetrdelkdyREKLEKLKRE 400
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 46048213    216 KENLQGLVSRQTFIIQELEKQLSRATNNNSILQKQQLELMDTV 258
Cdd:TIGR02169  401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
55-240 4.82e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 41.62  E-value: 4.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   55 RESATEQYNTNALQRDAphvepdfSSQKLQHLEHVMENYTQWLQKLENYIVENmKSEMAQIQQNAVQNHTAtmLEIGTSL 134
Cdd:COG1196  795 LEELEEELEEAERRLDA-------LERELESLEQRRERLEQEIEELEEEIEEL-EEKLDELEEELEELEKE--LEELKEE 864
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213  135 LSQTAEQTRKLTDvetqvlnqtsrlEIQLLENSLStyKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGKHKEELDTLKE 214
Cdd:COG1196  865 LEELEAEKEELED------------ELKELEEEKE--ELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPE 930
                        170       180
                 ....*....|....*....|....*.
gi 46048213  215 EKENLQGLvsRQTFIIQELEKQLSRA 240
Cdd:COG1196  931 LEEELEEE--YEDTLETELEREIERL 954
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
82-250 4.86e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 41.62  E-value: 4.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   82 KLQHLEHVMENYTQWLQKLEnYIVENMKSEMAQIQQnAVQNHTATMLEIGTSLLSQTAEQ---TRKLTDVETQ---VLNQ 155
Cdd:COG1196  233 KLKELRKELEELEEELSRLE-EELEELQEELEEAEK-EIEELKSELEELREELEELQEELlelKEEIEELEGEislLRER 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213  156 TSRLEIQLLENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKILEME---GKHKEELDTLKEEKENL-QGLVSRQTfiiq 231
Cdd:COG1196  311 LEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEeakEELEEKLSALLEELEELfEALREELA---- 386
                        170
                 ....*....|....*....
gi 46048213  232 ELEKQLSRATNNNSILQKQ 250
Cdd:COG1196  387 ELEAELAEIRNELEELKRE 405
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
79-256 6.06e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 6.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213     79 SSQKLQHLEHVMENYTQWLQKLENYIvENMKSEMAQIQQNAVQNHTATMLEIgTSLLSQTAEQTRKLTDVETQVlnqtSR 158
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRI-ENRLDELSQELSDASRKIGEIEKEI-EQLEQEEEKLKERLEELEEDL----SS 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    159 LEIQLLENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKILEmegkhkEELDTLKEEKENLQGLVSRQTFIIQELEKQLS 238
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH------SRIPEIQAELSKLEEEVSRIEARLREIEQKLN 822
                          170
                   ....*....|....*...
gi 46048213    239 RATNNNSILQKQQLELMD 256
Cdd:TIGR02169  823 RLTLEKEYLEKEIQELQE 840
RmuC COG1322
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and ...
91-253 7.81e-04

DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and repair];


Pssm-ID: 224241 [Multi-domain]  Cd Length: 448  Bit Score: 40.45  E-value: 7.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213  91 ENYTQWLQKLENyiVENMKSEMAQ-IQQNAVQNHTATMLE----IGTSLLSQTAEQTRKLTDVETQV--LNQTSRLEIQL 163
Cdd:COG1322  18 AFIRQLLLRLGR--LEQMLGELAAvLEQLLLLLAFRAEAEqlrtFARSLQALNLELIQELNELKARLqqQLLQSREQLQL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213 164 LENSLStyKLEKQLLQQTNEIL-----KIHEKNSLLEHKILEM---------------EGKHKEELDTLKEEKENLQGlv 223
Cdd:COG1322  96 LIESLA--QLSSEFQELANEIFeelnrRLAELNQQNLKQLLKPlrevlekfreqleqrIHESAEERSTLLEEIDRLLG-- 171
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 46048213 224 srqtfIIQELEKQ---LSRATNNN---SILQKQQLE 253
Cdd:COG1322 172 -----EIQQLAQEagnLTAALKGNktrGNWGEVQLE 202
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
173-267 1.22e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 292252 [Multi-domain]  Cd Length: 180  Bit Score: 38.72  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   173 LEKQLLQQTNEILKIHEKNSLLEHKIlemEGKHKEELDTLKEEKENLQGLVSRQTFIIQELEKQLSRATNNNS----ILQ 248
Cdd:pfam15619  79 LERKLKEKEAELLRLQDKLKKLKKLS---EDKNLAEREELQKKLEALEAKLEEKEEKIKELERQLELLEKNFRrqlaAEK 155
                          90
                  ....*....|....*....
gi 46048213   249 KQQLELMDTVHNLISLCTK 267
Cdd:pfam15619 156 KKTKEAQEEVKALQEEIER 174
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
77-261 1.27e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213     77 DFSSQKLQHLEHVMENYTQWLQKLENYIVE------NMKSEMAQIQQNavqnhtatmleigtsLLSQTAEQTRKltDVET 150
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEElrlevsELEEEIEELQKE---------------LYALANEISRL--EQQK 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    151 QVLNQtsrlEIQLLENSLSTYKLEKQLLQQTNEILKihEKNSLLEHKILEMEGKHKEELDTLKEEKENLQGLVSRqtfiI 230
Cdd:TIGR02168  305 QILRE----RLANLERQLEELEAQLEELESKLDELA--EELAELEEKLEELKEELESLEAELEELEAELEELESR----L 374
                          170       180       190
                   ....*....|....*....|....*....|.
gi 46048213    231 QELEKQLSRATNNNSILQKQQLELMDTVHNL 261
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASLNNEIERL 405
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
79-230 1.38e-03

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 38.84  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    79 SSQKLQHLEHVMENYTQ---------WLqkLENYIVENM--KSEMAQIQQnavqnhtatmlEIgTSLLSQTAEQTRKLTD 147
Cdd:TIGR04211  26 SGTPVTVLERSEDGYSRvrtpkgregWV--LSRYLSDTPsaRERLPELQQ-----------EL-AELQEELAELQEQLAE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   148 VETQvlNQTSRLEIQLLENSLSTYKLEKQLLQQTNE-ILKIHEKNSLLEHKILEMegkhKEELDTLKEEKENLQGLVSRQ 226
Cdd:TIGR04211  92 LRQE--NQELKQQLSTLEAELEELQKELERIKQISAnAIELDEENRELREELAEL----KQENEALEAENERLQENEQRR 165

                  ....
gi 46048213   227 TFII 230
Cdd:TIGR04211 166 WFLY 169
PRK10935 PRK10935
nitrate/nitrite sensor protein NarQ; Provisional
122-255 1.62e-03

nitrate/nitrite sensor protein NarQ; Provisional


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 39.45  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213  122 NHTATmlEIGT---SLLSQTAEQTRKLTDV--ETQVLNQTSRLeiqllensLSTYKLEKQLLQQTNEILKIHEKNSLLEH 196
Cdd:PRK10935 216 NQMSS--ELHKlyrSLEASVEEKTRKLTQAnrSLEVLYQCSQA--------LNASQIDVHCFRHILQIVRDHEGLDYLEL 285
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46048213  197 KILE------MEGKHKEELD----TLKEEKENL------QGLVSRQTFIIQELEKQLSRA-TNNNSILQKQQLELM 255
Cdd:PRK10935 286 EVGEnehwriSEGQPNPELPwqilPLTMEDTVLgylhwqASLPCPDEPLMNNVAQMLGRGlYFNQAQKQQQQLLLM 361
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
81-254 1.76e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.62  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    81 QKLQHLEHVMENYTQWLQKLENYIvENMKSEMAQI--------QQNAVQNHTATMLEIGTSLLSQTAEQTRKLTDVETQv 152
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQI-KKLQQEKELLekeierlkETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET- 468
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   153 lnQTSRLEIQLLENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKI----------------LEMEGKHKE-ELDTLKEE 215
Cdd:TIGR04523 469 --QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVkdltkkisslkekiekLESEKKEKEsKISDLEDE 546
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 46048213   216 KENLQGLVSRQTF--IIQELEKQLSRATNNNSILQKQQLEL 254
Cdd:TIGR04523 547 LNKDDFELKKENLekEIDEKNKEIEELKQTQKSLKKKQEEK 587
recN TIGR00634
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ...
81-263 2.04e-03

DNA repair protein RecN; All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273187 [Multi-domain]  Cd Length: 563  Bit Score: 39.33  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    81 QKLQHLEHVMENYTQWLQKLENYIVENMKSE---MAQIQqnavqnhtatmLEIGTSLLSQTAEQTRKLTDVETQVLNQTS 157
Cdd:TIGR00634 219 QRLSNLEKLRELSQNALAALRGDVDVQEGSLlegLGEAQ-----------LALASVIDGSLRELAEQVGNALTEVEEATR 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   158 RL-----EIQLLENSLStYKLEKQllqqtNEILKIHEKNSLLEHKILEMEGKHKEELDTLKEEKENLQGLVSRqtfiIQE 232
Cdd:TIGR00634 288 ELqnyldELEFDPERLN-EIEERL-----AQIKRLKRKYGASVEEVLEYAEKIKEELDQLDDSDESLEALEEE----VDK 357
                         170       180       190
                  ....*....|....*....|....*....|..
gi 46048213   233 LEKQLSRATNNNSILQKQQLE-LMDTVHNLIS 263
Cdd:TIGR00634 358 LEEELDKAAVALSLIRRKAAErLAKRVEQELK 389
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
81-263 2.45e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213     81 QKLQHLEHVMENYTQWLQKLENYIvENMKSEMAQIQQNAVQNHTATMLEIGTSLLSQTAEQTRKLTDVetQVLNQTSRLE 160
Cdd:TIGR02169  758 SELKELEARIEELEEDLHKLEEAL-NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL--TLEKEYLEKE 834
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    161 IQLLENSLSTYKLEKQLLQQTNEIL--KIHEKNSLLEHK---ILEMEGKH---KEELDTLKEEKENLQGLVSRQTFIIQE 232
Cdd:TIGR02169  835 IQELQEQRIDLKEQIKSIEKEIENLngKKEELEEELEELeaaLRDLESRLgdlKKERDELEAQLRELERKIEELEAQIEK 914
                          170       180       190
                   ....*....|....*....|....*....|.
gi 46048213    233 LEKQLSRATNNNSILQKQQLELMDTVHNLIS 263
Cdd:TIGR02169  915 KRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
89-216 2.50e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homologue in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 281941 [Multi-domain]  Cd Length: 218  Bit Score: 38.13  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    89 VMENYTQWLQKLE------NYIVENMKSEMAQIQQNAVQNHT-ATMLEigtSLLSQTAEQTRKLTDVETQVLNQTSR--- 158
Cdd:pfam04012  10 LRANIHEGLDKAEdpekmlEQAIRDMQSELGKARQALAQVIArQKQLE---RKLEEQKEQAKKLENKARAALTKGNEela 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46048213   159 ----LEIQLLENSLStyKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGKHKEELDTLKEEK 216
Cdd:pfam04012  87 realAEIATLEKLAE--ALETQLTQQRSAVEQLRKQLAALETKIQQLKAKKTALKARLKAAK 146
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
86-254 2.96e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 38.97  E-value: 2.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213  86 LEHVMENYTQWLQKLENYIVENMKSEMAQIQQNAVQnhTATMLEIGTSLLSQTAEQTRKLTDVETQVLNQTSRL--EIQL 163
Cdd:COG0419 194 LSELLEDIEDLLEALEEELKELKKLEEIQEEQEEEE--LEQEIEALEERLAELEEEKERLEELKARLLEIESLEleALKI 271
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213 164 LENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGKH----KEELDTLKEEKENLQGLVSRQTFIIQELEKQLSR 239
Cdd:COG0419 272 REEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALleelEELLEKLKSLEERLEKLEEKLEKLESELEELAEE 351
                       170
                ....*....|....*
gi 46048213 240 ATNNNSILQKQQLEL 254
Cdd:COG0419 352 KNELAKLLEERLKEL 366
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
165-285 3.04e-03

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


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 38.12  E-value: 3.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213 165 ENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGKhKEELDTLKEEKENLQGLVSRQTFIIQELEKQLSRATNNN 244
Cdd:COG1579   4 NNLKSLLAIQKLDLEKDRLEPRIKEIRKALKKAKAELEAL-NKALEALEIELEDLENQVSQLESEIQEIRERIKRAEEKL 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213 245 S----------------ILQKQQLELMDT---VHNLISLCTKEGVLLKGGKREEEKPFRD 285
Cdd:COG1579  83 SavkderelralnieiqIAKERINSLEDElaeLMEEIEKLEKEIEDLKERLERLEKNLAE 142
CortBP2 pfam09727
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ...
66-235 3.69e-03

Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.


Pssm-ID: 286770 [Multi-domain]  Cd Length: 187  Bit Score: 37.17  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    66 ALQRDAphvepdFSSQKLQHLEHVMEN-YTQWLQKLENYIV--ENMKSEMAQIQQNAVQNHTATMLEigtsllsqtaeqt 142
Cdd:pfam09727  53 ALQRDS------ELAAGQSTDEDVYKQiYENPLAELEKLIEkqKRTQRRMLEQLLAAEKRHRRVLEE------------- 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   143 rkltdvetqvLNQTSRLEIQLLENSLS-TYKLEK---QLLQQTneilkIHEKnslLEHKILEMEgkHKEELDTLKEEKEN 218
Cdd:pfam09727 114 ----------LEEEKRKHAQDTAQGDDfTNLLEKereRLKQLL-----EQEK---AYQKRLEKE--LEKLLEKLEEELTR 173
                         170
                  ....*....|....*..
gi 46048213   219 LQGLVSrqtFIIQELEK 235
Cdd:pfam09727 174 LKQFAL---LLVKERKR 187
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
154-254 3.88e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.46  E-value: 3.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   154 NQTSRLEIQLLENSLSTYKLEKQLLQQT-----NEILKIH----------EKNSLLEHKILEMEGKHKEELDTLKEEKEN 218
Cdd:TIGR04523 161 YNDLKKQKEELENELNLLEKEKLNIQKNidkikNKLLKLElllsnlkkkiQKNKSLESQISELKKQNNQLKDNIEKKQQE 240
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 46048213   219 LQGLVSRQTFIIQELEKQLSRATNNNSILQKQQLEL 254
Cdd:TIGR04523 241 INEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
PRK12704 PRK12704
phosphodiesterase; Provisional
139-235 3.90e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 3.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213  139 AEQTRK--LTDVETQVLNQTSRLEIQLLE--NSLStyKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGKHKEELDTLKE 214
Cdd:PRK12704  51 AEAIKKeaLLEAKEEIHKLRNEFEKELRErrNELQ--KLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEK 128
                         90       100
                 ....*....|....*....|.
gi 46048213  215 EKENLQGLVSRQtfiIQELEK 235
Cdd:PRK12704 129 KEEELEELIEEQ---LQELER 146
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
137-239 4.04e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 283261 [Multi-domain]  Cd Length: 660  Bit Score: 38.17  E-value: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   137 QTAEQTRKLTDV--ETQVLNQTSRLEIQLLENSLSTYKLEKQLLQQTNEILKihEKNSLLEhkilemEGKHKEELDTLKE 214
Cdd:pfam05557 377 QLLERIEEAEDMtqKMQAHNEEMEAQLSVAEEELGGYKQRAQTLERELQALR--QQESLAD------PSSSKEEVDSLRR 448
                          90       100
                  ....*....|....*....|....*
gi 46048213   215 EKENLQGLVSRQTFIIQELEKQLSR 239
Cdd:pfam05557 449 KLEELELERQRLREQKNELEMELER 473
PRK12704 PRK12704
phosphodiesterase; Provisional
172-254 5.91e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.84  E-value: 5.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213  172 KLEKQLLQQTNEILKiheknslLEHKILEMEGKHKEELDTLKEEKENLQGLVSRQTFIIQELEKQLSRATNnnsILQKQQ 251
Cdd:PRK12704  72 EFEKELRERRNELQK-------LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE---LIEEQL 141

                 ...
gi 46048213  252 LEL 254
Cdd:PRK12704 142 QEL 144
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
81-240 6.54e-03

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


Pssm-ID: 292293 [Multi-domain]  Cd Length: 211  Bit Score: 36.58  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213    81 QKLQHLEHVMENYT----QWLQKLENYivenmKSEMAQIQQNAVQNHTATMLEIGTSLLSQTAEQTRKLTDVeTQVLNQT 156
Cdd:pfam15665  53 QRIQTLEECLEQHEkekrQALAEFEVY-----KRRVEERELKLEAEHSQRVVALSREVEEAKRDFEEKLRSF-AQLQQQL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213   157 SRLEIQLLENSLSTYKLEKQLLQQTNEilkihEKNSLLEHKILEMEGKHKEELDTLKEEKENLQGLVSRqtfIIQELEKQ 236
Cdd:pfam15665 127 EAEKEAALEELRAKHRQEIEELLKTQQ-----AQRSSSLKEQEKLEEKHKAEVESLRQEVEDLRQEKKK---LVEEYEQK 198

                  ....
gi 46048213   237 LSRA 240
Cdd:pfam15665 199 LSKA 202
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
109-263 6.92e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 37.77  E-value: 6.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213  109 KSEMAQIQQNavqnhtatmLEIGTSLLSQTAEQTRKLTDVETQVL------NQTSRLEIQLLENSLstYKLEKQLLQQTN 182
Cdd:COG1196  178 ERKLERTEEN---------LERLEDLLEELEKQLEKLERQAEKAEryqelkAELRELELALLLAKL--KELRKELEELEE 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213  183 EILKIHEKNSLLEHKILEME---GKHKEELDTLKEEKENLQGLVSRQTFIIQELEKQLSRATNNNSILQKQQLELMDTVH 259
Cdd:COG1196  247 ELSRLEEELEELQEELEEAEkeiEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLE 326

                 ....
gi 46048213  260 NLIS 263
Cdd:COG1196  327 ELKE 330
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
98-275 7.46e-03

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 224337 [Multi-domain]  Cd Length: 407  Bit Score: 37.32  E-value: 7.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213  98 QKLENYIVENMKSEMAQIQQ----NAV---QNHTATMLEIGtSLLSQTAEQTRKLT-------DVETQVLNQTSRLEIQL 163
Cdd:COG1419   1 MKIKKFTAESMREAIEKIRKelgeDAVilsNRRIKKGGFLG-LLFSKTAVEVTKLAavdselrKFQTREAAKVKDAEAQL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213 164 LENSLSTYKLEKQLLQ------------QTNEI----LKIHEKNSLLEHKILEMEGKHKEELDTLKEEKENLQGLVSRQT 227
Cdd:COG1419  80 LKDPAEKKREERKAAKkierstpslierKTQEVkdsgEEIAEMMRDEKVPIRELEEIPPEFVALYKQEIQSPTRLNLINE 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 46048213 228 FIIQELEKQLSRATNNNsilQKQQLELMDTVHNLISLCTKEGVLLKGG 275
Cdd:COG1419 160 LLRAGLELEILDMKDES---YEDLRYFSEKLRKLLLSLIENLIVEQKR 204
RloC COG4694
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
54-241 8.30e-03

Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227038 [Multi-domain]  Cd Length: 758  Bit Score: 37.22  E-value: 8.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213  54 CRESATEQYNTNALQRDAPHVEPDFSSQklqHLEHVMENYTQWLQKLENYIVENMKSEMAQIQQNAVQNHTATMLEIGTS 133
Cdd:COG4694 327 NLTKIALERLDEIACTEAWKDQTDLDTE---NLKNIIETLRSKRLANQAKMLDKSKEMSRNFKLDSTKDEIDAIKDLIKK 403
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048213 134 LLSQTAEQTRKLTDVETQVLNQTSRLEIQLLENSlstykleKQLLQQTNEILKIHEKNSLLEHKILEMegkhKEELDTLK 213
Cdd:COG4694 404 ANAQVVNHNERIKNFEKQKKSSKEQLEKFLVNEF-------KSDVQEYNKYCGLEKKINNLEKEIKNN----QEEVKKLS 472
                       170       180
                ....*....|....*....|....*...
gi 46048213 214 EEKENLQGLVSRQTFIIQELEKQLSRAT 241
Cdd:COG4694 473 NEIKEIEKFLVSIKPIVKEINQTLLKGY 500
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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