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Conserved domains on  [gi|41327691|ref|NP_078980|]
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kinesin-like protein KIF16B isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 2-365 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


:

Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 558.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    2 ASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKT 81
Cdd:cd01365    1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRwDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365   80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  162 L-RRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE- 239
Cdd:cd01365  159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqDAANTLAKKKQVFVPYRDSVLTWL 318
Cdd:cd01365  239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALA----DMSSGKSKKKSSFIPYRDSVLTWL 314

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 41327691  319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365  315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
 446-562 1.53e-78

forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


:

Pssm-ID: 438784 [Multi-domain]  Cd Length: 117  Bit Score: 253.70  E-value: 1.53e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22732    1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 41327691  526 GVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22732   81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
 1184-1311 3.53e-78

The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


:

Pssm-ID: 132784  Cd Length: 127  Bit Score: 253.07  E-value: 3.53e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691 1184 IKISIPRYVLCGQGKDAHFEFEVKITVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSH 1263
Cdd:cd06874    1 IKITIPRYVLRGQGKDEHFEFEVKITVLDETWTVFRRYSRFRELHKTMKLKYPEVAALEFPPKKLFGNKSERVAKERRRQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 41327691 1264 LEKYLRDFFSVMLQSATSPLHiNKVGLTLSKHTICEFSPFFKKGVFDY 1311
Cdd:cd06874   81 LETYLRNFFSVCLKLPACPLY-PKVGRTLSKATLCDFSPFFRKGVFEN 127
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 595-1078 7.72e-16

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 83.06  E-value: 7.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  595 GLEFERQQREELE-KLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLL 673
Cdd:COG1196  303 DIARLEERRRELEeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  674 AEKEKFEEERLReqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEE 753
Cdd:COG1196  383 ELAEELLEALRA-----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  754 QEKEQVMLVAHLEEQLREKQEMIQLLR-RGEVQWVEEEKRDLEGIRESLLR-VKEARAGGDEDGEELEKAQLRFFEFKRR 831
Cdd:COG1196  458 EEALLELLAELLEEAALLEAALAELLEeLAEAAARLLLLLEAEADYEGFLEgVKAALLLAGLRGLAGAVAVLIGVEAAYE 537

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  832 QLV----------KLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDfekikPVEYR 901
Cdd:COG1196  538 AALeaalaaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD-----LREAD 612

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  902 LQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLdnTLYQVEKEMEEKEEQLAQYQANANQLQKLQATfeftANIAR 981
Cdd:COG1196  613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV--TLEGEGGSAGGSLTGGSRRELLAALLEAEAEL----EELAE 686

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  982 QEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLAslnsgsrEQSGLQASLEAEQEALE 1061
Cdd:COG1196  687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL-------EEEELLEEEALEELPEP 759

                        490
                 ....*....|....*..
gi 41327691 1062 KDQERLEYEIQQLKQKI 1078
Cdd:COG1196  760 PDLEELERELERLEREI 776
Kinesin_assoc super family cl24686
Kinesin-associated;
364-476 3.07e-11

Kinesin-associated;


The actual alignment was detected with superfamily member pfam16183:

Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 63.71  E-value: 3.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    364 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 394
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    395 ---LLDSPTALSMEEKLQQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 462
Cdd:pfam16183   83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162

                          170
                   ....*....|....
gi 41327691    463 LLSTGIILYHLKEG 476
Cdd:pfam16183  163 PLMSECLLYYIKDG 176
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 2-365 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 558.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    2 ASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKT 81
Cdd:cd01365    1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRwDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365   80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  162 L-RRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE- 239
Cdd:cd01365  159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqDAANTLAKKKQVFVPYRDSVLTWL 318
Cdd:cd01365  239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALA----DMSSGKSKKKSSFIPYRDSVLTWL 314

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 41327691  319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365  315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 3-365 6.70e-151

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 458.57  E-value: 6.70e-151
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691       3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGgtgdsgRERTKTFTYDFSFysadtksPDYVSQEMVFKTL 82
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKN------RQGEKKFTFDKVF-------DATASQEDVFEET 67

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691      83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLL 162
Cdd:smart00129   68 AAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE--EGWQFSVKVSYLEIYNEKIRDLL 145

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691     163 RRKSSKtfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPC 242
Cdd:smart00129  146 NPSSKK---LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGS 222

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691     243 ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdaantlakkKQVFVPYRDSVLTWLLKDS 322
Cdd:smart00129  223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDS 292

                           330       340       350       360
                    ....*....|....*....|....*....|....*....|...
gi 41327691     323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:smart00129  293 LGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
9-358 1.20e-149

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 454.72  E-value: 1.20e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691      9 RVRPMNRREKDLEAKFIIQMEKSKTTITNLKIpeggtgDSGRERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVK 88
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVESSH------LTNKNRTKTFTFDKVFDPEAT-------QEDVYEETAKPLVE 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691     89 SAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSK 168
Cdd:pfam00225   68 SVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK--ERSEFSVKVSYLEIYNEKIRDLLSPSNKN 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    169 TFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPCE-TVSK 247
Cdd:pfam00225  146 KRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGK 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    248 IHLVDLAGSERADATG-ATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTWLLKDSLGGN 326
Cdd:pfam00225  226 LNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----------KKSKHIPYRDSKLTRLLQDSLGGN 294

                          330       340       350
                   ....*....|....*....|....*....|..
gi 41327691    327 SKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:pfam00225  295 SKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
27-508 7.22e-80

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 274.69  E-value: 7.22e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   27 QMEKSKTTITNLKIPEGGTGDSGRER-----------TKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYN 95
Cdd:COG5059   18 EKSVSDIKSTIRIIPGELGERLINTSkkshvslekskEGTYAFDKVFGPSAT-------QEDVYEETIKPLIDSLLLGYN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   96 ACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINEttRWDEASFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVR 175
Cdd:COG5059   91 CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLED--LSMTKDFAVSISYLEIYNEKIYDLL---SPNEESLNIR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  176 EHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDSEMPCETVSKIHLVDLAG 255
Cdd:COG5059  166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELASKNKVSGTSETSKLSLVDLAG 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  256 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlaKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 335
Cdd:COG5059  244 SERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  336 SPADVNYGETLSTLRYANRAKNIINKPTINEDANVKL--------IRELRAEIARLKTLLAQGNQIALLDSPTA--LSME 405
Cdd:COG5059  314 SPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSQSSLSGIFAymQSLK 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  406 EKLQQNEARVQELTKEWTNKWNETQNILKEQTLALRKEG---------IGVVLDSELPHLIGIDDDLLSTGIILYHLKEG 476
Cdd:COG5059  394 KETETLKSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLqflrieidrLLLLREEELSKKKTKIHKLNKLRHDLSSLLSS 473

                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 41327691  477 QT-----YVGRDDASTEQDIVLHGLDLES--EHCIFENI 508
Cdd:COG5059  474 IPeetsdRVESEKASKLRSSASTKLNLRSsrSHSKFRDH 512
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
 446-562 1.53e-78

forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438784 [Multi-domain]  Cd Length: 117  Bit Score: 253.70  E-value: 1.53e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22732    1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 41327691  526 GVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22732   81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
 1184-1311 3.53e-78

The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132784  Cd Length: 127  Bit Score: 253.07  E-value: 3.53e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691 1184 IKISIPRYVLCGQGKDAHFEFEVKITVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSH 1263
Cdd:cd06874    1 IKITIPRYVLRGQGKDEHFEFEVKITVLDETWTVFRRYSRFRELHKTMKLKYPEVAALEFPPKKLFGNKSERVAKERRRQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 41327691 1264 LEKYLRDFFSVMLQSATSPLHiNKVGLTLSKHTICEFSPFFKKGVFDY 1311
Cdd:cd06874   81 LETYLRNFFSVCLKLPACPLY-PKVGRTLSKATLCDFSPFFRKGVFEN 127
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 4-392 1.03e-73

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 269.88  E-value: 1.03e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691     4 VKVAVRVRPMNrreKDLEAKFIIQ-MEKSKTTITNlkipeggtgdsgrertKTFTYDfsfYSADTKSpdyvSQEMVFKTL 82
Cdd:PLN03188  100 VKVIVRMKPLN---KGEEGEMIVQkMSNDSLTING----------------QTFTFD---SIADPES----TQEDIFQLV 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN---------SGDS-GLIPRICEGLFSRINE-----TTRwdEASFRTE 147
Cdd:PLN03188  154 GAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPanglleehlSGDQqGLTPRVFERLFARINEeqikhADR--QLKYQCR 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   148 VSYLEIYNERVRDLLRrKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:PLN03188  232 CSFLEIYNEQITDLLD-PSQK--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVF 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   228 TIKFtqakfdsEMPCETV---------SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAan 298
Cdd:PLN03188  309 TCVV-------ESRCKSVadglssfktSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG-- 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   299 tlakkKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DANV--KL 372
Cdd:PLN03188  380 -----KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEV 454

                         410       420
                  ....*....|....*....|
gi 41327691   373 IRELRAEIARLKtllAQGNQ 392
Cdd:PLN03188  455 IRQLRDELQRVK---ANGNN 471
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 595-1078 7.72e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 83.06  E-value: 7.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  595 GLEFERQQREELE-KLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLL 673
Cdd:COG1196  303 DIARLEERRRELEeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  674 AEKEKFEEERLReqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEE 753
Cdd:COG1196  383 ELAEELLEALRA-----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  754 QEKEQVMLVAHLEEQLREKQEMIQLLR-RGEVQWVEEEKRDLEGIRESLLR-VKEARAGGDEDGEELEKAQLRFFEFKRR 831
Cdd:COG1196  458 EEALLELLAELLEEAALLEAALAELLEeLAEAAARLLLLLEAEADYEGFLEgVKAALLLAGLRGLAGAVAVLIGVEAAYE 537

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  832 QLV----------KLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDfekikPVEYR 901
Cdd:COG1196  538 AALeaalaaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD-----LREAD 612

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  902 LQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLdnTLYQVEKEMEEKEEQLAQYQANANQLQKLQATfeftANIAR 981
Cdd:COG1196  613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV--TLEGEGGSAGGSLTGGSRRELLAALLEAEAEL----EELAE 686

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  982 QEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLAslnsgsrEQSGLQASLEAEQEALE 1061
Cdd:COG1196  687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL-------EEEELLEEEALEELPEP 759

                        490
                 ....*....|....*..
gi 41327691 1062 KDQERLEYEIQQLKQKI 1078
Cdd:COG1196  760 PDLEELERELERLEREI 776
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 592-926 8.69e-13

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: 72.85  E-value: 8.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    592 YNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEivqlQIRKQEESLKRRSFHIEnKLKD 671
Cdd:pfam17380  260 YNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKARQAEMD-RQAA 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    672 LLAEKEKFEEERLREQQEIELQKKRQEEETfLRVQE---ELQRLKELnnnekaekfqifqELDQLQKEKDEQYAKLELEK 748
Cdd:pfam17380  335 IYAEQERMAMERERELERIRQEERKRELER-IRQEEiamEISRMREL-------------ERLQMERQQKNERVRQELEA 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    749 KR----LEEQEKEQVMLVAHLEEQLREKQEMIqllRRGEVQWVEEEK-RDLEGIRESLLRVKEARAGGDEDGEELEKAQL 823
Cdd:pfam17380  401 ARkvkiLEEERQRKIQQQKVEMEQIRAEQEEA---RQREVRRLEEERaREMERVRLEEQERQQQVERLRQQEEERKRKKL 477

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    824 RFFEFKRRQlvklvnlEKDLVQQKDILKKEVQEEQEILeclkCEHDKESRLLEKHDESVTdvTEVPQDFEKIKPVEYRLQ 903
Cdd:pfam17380  478 ELEKEKRDR-------KRAEEQRRKILEKELEERKQAM----IEEERKRKLLEKEMEERQ--KAIYEEERRREAEEERRK 544

                          330       340
                   ....*....|....*....|...
gi 41327691    904 YKERQLQYLLQNHLPTLLEEKQR 926
Cdd:pfam17380  545 QQEMEERRRIQEQMRKATEERSR 567
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 1212-1269 5.37e-12

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 62.64  E-value: 5.37e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 41327691   1212 DETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYLR 1269
Cdd:pfam00787    6 LEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQ 63
PTZ00121 PTZ00121
MAEBL; Provisional
 599-859 1.37e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 69.78  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   599 ERQQREELEKLESKRKLIE--EMEEKQKSD---KAELERMQQE---VETQRKETEIVQLQIRKQEESLKRRSFHIENKLK 670
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEakKAEEKKKADelkKAEELKKAEEkkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   671 dLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQyaKLELEKKR 750
Cdd:PTZ00121 1600 -LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK--KAEEDKKK 1676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   751 LEEQEKEQVMLVAHLEEQLREKQEM--IQLLRRGEvqwvEEEKRDLEGIR----ESLLRVKEARAGGDEDGEELEKAQLR 824
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAkkAEELKKKE----AEEKKKAEELKkaeeENKIKAEEAKKEAEEDKKKAEEAKKD 1752

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 41327691   825 FFEFKRRQLVKLVNLEKDLVQQKD---ILKKEVQEEQE 859
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEkeaVIEEELDEEDE 1790
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 1197-1269 1.67e-11

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 61.98  E-value: 1.67e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41327691    1197 GKDAHFEFEVKITVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFG---NKDERVIAERRSHLEKYLR 1269
Cdd:smart00312   10 GKHYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGrlnNFSEEFIEKRRRGLEKYLQ 85
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 597-894 3.06e-11

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: 68.16  E-value: 3.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    597 EFERQQREELEKLESKRKLIEEMEEkqksdkaELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLAEK 676
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEE-------EIEELQKELYALANEISRLEQQKQILRERLAN----LERQLEELEAQL 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    677 EKFEEERLREQQEIELQKKRQEEetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 756
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEE-----LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    757 EQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKL 836
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 41327691    837 VNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRlLEKHDESVTDVTEVPQDFEK 894
Cdd:TIGR02168  481 ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG-LSGILGVLSELISVDEGYEA 537
Kinesin_assoc pfam16183
Kinesin-associated;
364-476 3.07e-11

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 63.71  E-value: 3.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    364 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 394
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    395 ---LLDSPTALSMEEKLQQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 462
Cdd:pfam16183   83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162

                          170
                   ....*....|....
gi 41327691    463 LLSTGIILYHLKEG 476
Cdd:pfam16183  163 PLMSECLLYYIKDG 176
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
471-551 3.46e-07

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 49.57  E-value: 3.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  471 YHLKEGQTYVGRDDASteqDIVLHGLDLESEHCIFENIGGTVTLIPLsGSQ--CSVNGVQIVEATHLNQGAVILLGRTnM 548
Cdd:COG1716   16 FPLDGGPLTIGRAPDN---DIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRLGKT-E 90


                 ...
gi 41327691  549 FRF 551
Cdd:COG1716   91 LRF 93
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
 471-555 1.28e-05

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 44.94  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    471 YHLKEGQTYVGRDDastEQDIVLHGLDLESEHCIFENIGGTVTLIPL-SGSQCSVNGVQIVEATH-LNQGAVILLGRTnM 548
Cdd:pfam16697   12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDLgSGNGTLVNGQRVTELGIaLRPGDRIELGQT-E 87


                   ....*..
gi 41327691    549 FRFNHPK 555
Cdd:pfam16697   88 FCLVPAD 94
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 607-807 6.52e-03

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: 40.25  E-value: 6.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  607 EKLESKRKLIEEMEEKqksdKAELERMQQEVETQRKETEIVQLqIRKQEESLKRRSFHIENKLKDLLAEKEKFeeerlre 686
Cdd:cd16269   87 EDQKFQKKLMEQLEEK----KEEFCKQNEEASSKRCQALLQEL-SAPLEEKISQGSYSVPGGYQLYLEDREKL------- 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  687 qqeieLQKKRQEEETFLRVQEELQR-LKELNNNEKAEKfQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHL 765
Cdd:cd16269  155 -----VEKYRQVPRKGVKAEEVLQEfLQSKEAEAEAIL-QADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKL 228

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 41327691  766 EEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEA 807
Cdd:cd16269  229 EDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEA 270
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 2-365 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 558.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    2 ASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTGDSgRERTKTFTYDFSFYSADTKSPDYVSQEMVFKT 81
Cdd:cd01365    1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKAT-REVPKSFSFDYSYWSHDSEDPNYASQEQVYED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRwDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd01365   80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTN-QNMSYSVEVSYMEIYNEKVRDL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  162 L-RRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE- 239
Cdd:cd01365  159 LnPKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAEt 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  240 -MPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqDAANTLAKKKQVFVPYRDSVLTWL 318
Cdd:cd01365  239 nLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALA----DMSSGKSKKKSSFIPYRDSVLTWL 314

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 41327691  319 LKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:cd01365  315 LKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 3-365 6.70e-151

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 458.57  E-value: 6.70e-151
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691       3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGgtgdsgRERTKTFTYDFSFysadtksPDYVSQEMVFKTL 82
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKN------RQGEKKFTFDKVF-------DATASQEDVFEET 67

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691      83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLL 162
Cdd:smart00129   68 AAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE--EGWQFSVKVSYLEIYNEKIRDLL 145

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691     163 RRKSSKtfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPC 242
Cdd:smart00129  146 NPSSKK---LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGS 222

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691     243 ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSqdaantlakkKQVFVPYRDSVLTWLLKDS 322
Cdd:smart00129  223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----------KSRHIPYRDSKLTRLLQDS 292

                           330       340       350       360
                    ....*....|....*....|....*....|....*....|...
gi 41327691     323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTIN 365
Cdd:smart00129  293 LGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
9-358 1.20e-149

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 454.72  E-value: 1.20e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691      9 RVRPMNRREKDLEAKFIIQMEKSKTTITNLKIpeggtgDSGRERTKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVK 88
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVDSETVESSH------LTNKNRTKTFTFDKVFDPEAT-------QEDVYEETAKPLVE 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691     89 SAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVRDLLRRKSSK 168
Cdd:pfam00225   68 SVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK--ERSEFSVKVSYLEIYNEKIRDLLSPSNKN 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    169 TFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPCE-TVSK 247
Cdd:pfam00225  146 KRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESvKTGK 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    248 IHLVDLAGSERADATG-ATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTWLLKDSLGGN 326
Cdd:pfam00225  226 LNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----------KKSKHIPYRDSKLTRLLQDSLGGN 294

                          330       340       350
                   ....*....|....*....|....*....|..
gi 41327691    327 SKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:pfam00225  295 SKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 3-356 1.69e-140

Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 430.91  E-value: 1.69e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLKIPEGGTgdsgrertKTFTYDFSFYSADTkspdyvsQEMVFKTL 82
Cdd:cd00106    1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDPPKNRVAPP--------KTFAFDAVFDSTST-------QEEVYEGT 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS-GLIPRICEGLFSRINETtRWDEASFRTEVSYLEIYNERVRDL 161
Cdd:cd00106   66 AKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPDPEQrGIIPRALEDIFERIDKR-KETKSSFSVSASYLEIYNEKIYDL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  162 LRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMP 241
Cdd:cd00106  145 LSPVPKK--PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGE 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTWLLKD 321
Cdd:cd00106  223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----------GQNKHIPYRDSKLTRLLQD 291

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 41327691  322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd00106  292 SLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 3-358 9.02e-118

Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 370.64  E-value: 9.02e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnLKIPEGGTGdsgrERTKTFTYDfSFYSADTKspdyvsQEMVFKTL 82
Cdd:cd01371    2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVS-VRNPKATAN----EPPKTFTFD-AVFDPNSK------QLDVYDET 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNERVR 159
Cdd:cd01371   70 ARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQ--NNQQFLVRVSYLEIYNEEIR 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  160 DLLRRKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF--D 237
Cdd:cd01371  148 DLLGKDQTK--RLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgeD 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  238 SEMPCeTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLTW 317
Cdd:cd01371  226 GENHI-RVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----------GKSTHIPYRDSKLTR 293

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 41327691  318 LLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01371  294 LLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 3-358 1.11e-114

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 362.42  E-value: 1.11e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    3 SVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkipeggtgdsgRERTKTFTYDFSFysaDTKSPdyvsQEMVFKTL 82
Cdd:cd01372    2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVT-------------VGTDKSFTFDYVF---DPSTE----QEEVYNTC 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS------GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01372   62 VAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYTAEedeeqvGIIPRAIQHIFKKIEKKK--DTFEFQLKVSFLEIYNE 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  157 RVRDLLRRKSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKF 236
Cdd:cd01372  140 EIRDLLDPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKK 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  237 DSEMPC--------ETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAAntlakkkqvFV 308
Cdd:cd01372  220 NGPIAPmsaddknsTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGA---------HV 290

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 41327691  309 PYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01372  291 PYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 3-358 7.41e-104

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276821 [Multi-domain]  Cd Length: 345  Bit Score: 333.16  E-value: 7.41e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    3 SVKVAVRVRPMNRREKDLEAKFIIQ-MEKS------KTTITNLKIPEGGTGDSGRERTKTFTYDFsfysaDTKSPDYVSQ 75
Cdd:cd01370    1 SLTVAVRVRPFSEKEKNEGFRRIVKvMDNHmlvfdpKDEEDGFFHGGSNNRDRRKRRNKELKYVF-----DRVFDETSTQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   76 EMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYN 155
Cdd:cd01370   76 EEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLK--DEKEFEVSMSYLEIYN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  156 ERVRDLLRrKSSKTfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQ-A 234
Cdd:cd01370  154 ETIRDLLN-PSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQqD 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  235 KFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLsqdaantlaKKKQVFVPYRDSV 314
Cdd:cd01370  231 KTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADP---------GKKNKHIPYRDSK 301

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 41327691  315 LTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01370  302 LTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 4-367 1.05e-101

Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276824 [Multi-domain]  Cd Length: 347  Bit Score: 327.54  E-value: 1.05e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    4 VKVAVRVRPMNRREKDLEAKFIIQMEkSKTTITNLKIPEggtgdsgrertKTFTYDfSFYSADTkspdyvSQEMVFKTLG 83
Cdd:cd01373    3 VKVFVRIRPPAEREGDGEYGQCLKKL-SSDTLVLHSKPP-----------KTFTFD-HVADSNT------NQESVFQSVG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNS--------GDSGLIPRICEGLFSRIN--ETTRWDEASFRTEVSYLEI 153
Cdd:cd01373   64 KPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSesdnesphGLRGVIPRIFEYLFSLIQreKEKAGEGKSFLCKCSFLEI 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  154 YNERVRDLLRRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQ 233
Cdd:cd01373  144 YNEQIYDLLDPASR---NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  234 AKFDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDaantlakkKQVFVPYRDS 313
Cdd:cd01373  221 WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHG--------KQRHVCYRDS 292

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 41327691  314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01373  293 KLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 3-358 2.22e-101

Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276825 [Multi-domain]  Cd Length: 321  Bit Score: 325.44  E-value: 2.22e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    3 SVKVAVRVRPMNRREKDLEAKFIiqMEKSKTTITNLKIPEGgtgdsgrertkTFTYDFSFysaDTKSPDYVsqemVFKTL 82
Cdd:cd01374    1 KITVTVRVRPLNSREIGINEQVA--WEIDNDTIYLVEPPST-----------SFTFDHVF---GGDSTNRE----VYELI 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRWDeasFRTEVSYLEIYNERVRDLL 162
Cdd:cd01374   61 AKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDRE---FLLRVSYLEIYNEKINDLL 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  163 rrkSSKTFNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIK-FTQAKFDSEMP 241
Cdd:cd01374  138 ---SPTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITiESSERGELEEG 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  242 CETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlaKKKQVFVPYRDSVLTWLLKD 321
Cdd:cd01374  215 TVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE----------GKVGGHIPYRDSKLTRILQP 284

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 41327691  322 SLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01374  285 SLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 9-360 1.30e-98

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276817 [Multi-domain]  Cd Length: 329  Bit Score: 318.38  E-value: 1.30e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    9 RVRPMNRREKDLEAKFI-IQMEKSKTTITNlkipeggtgdSGRERTKTFTYDFSFysadtkSPDyVSQEMVFKTLGTdVV 87
Cdd:cd01366    9 RVRPLLPSEENEDTSHItFPDEDGQTIELT----------SIGAKQKEFSFDKVF------DPE-ASQEDVFEEVSP-LV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   88 KSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRWDeASFRTEVSYLEIYNERVRDLLRRKSS 167
Cdd:cd01366   71 QSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKG-WSYTIKASMLEIYNETIRDLLAPGNA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  168 KTFNLRVREHPKEGP-YVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKF------TQAKfdsem 240
Cdd:cd01366  150 PQKKLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIsgrnlqTGEI----- 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  241 pceTVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaantlakKKQVFVPYRDSVLTWLLK 320
Cdd:cd01366  225 ---SVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------------QKQSHIPYRNSKLTYLLQ 289

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 41327691  321 DSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIIN 360
Cdd:cd01366  290 DSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 1-358 1.94e-98

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 317.73  E-value: 1.94e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    1 MASVKVAVRVRPMNRREKDLEAKFIIqmekskttitnlKIPEGGTGD-SGRERTKTFTYDFSFYSADTkspdyvsQEMVF 79
Cdd:cd01369    1 ECNIKVVCRFRPLNELEVLQGSKSIV------------KFDPEDTVViATSETGKTFSFDRVFDPNTT-------QEDVY 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   80 KTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDS---GLIPRICEGLFSRINETTrwDEASFRTEVSYLEIYNE 156
Cdd:cd01369   62 NFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMD--ENLEFHVKVSYFEIYME 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  157 RVRDLLrrKSSKTfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAkf 236
Cdd:cd01369  140 KIRDLL--DVSKT-NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE-- 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  237 DSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVLT 316
Cdd:cd01369  215 NVETEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----------GKKTHIPYRDSKLT 283

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 41327691  317 WLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNI 358
Cdd:cd01369  284 RILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 1-367 9.17e-88

Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276815 [Multi-domain]  Cd Length: 353  Bit Score: 289.23  E-value: 9.17e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    1 MASVKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITnlkIPEGGTGDSGRerTKTFTYDFSFYSAdtkspdyVSQEMVFK 80
Cdd:cd01364    1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVS---VRTGGLADKSS--TKTYTFDMVFGPE-------AKQIDVYR 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   81 TLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN-----------SGDSGLIPRICEGLFSRINETtrwdEASFRTEVS 149
Cdd:cd01364   69 SVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDrspneeytwelDPLAGIIPRTLHQLFEKLEDN----GTEYSVKVS 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  150 YLEIYNERVRDLLRRKSSKTFNLRVREHP--KEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:cd01364  145 YLEIYNEELFDLLSPSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVF 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  228 TIKFTQAKFDSEMpcETV---SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakkK 304
Cdd:cd01364  225 SITIHIKETTIDG--EELvkiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------------R 290

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41327691  305 QVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINED 367
Cdd:cd01364  291 APHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
27-508 7.22e-80

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 274.69  E-value: 7.22e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   27 QMEKSKTTITNLKIPEGGTGDSGRER-----------TKTFTYDFSFYSADTkspdyvsQEMVFKTLGTDVVKSAFEGYN 95
Cdd:COG5059   18 EKSVSDIKSTIRIIPGELGERLINTSkkshvslekskEGTYAFDKVFGPSAT-------QEDVYEETIKPLIDSLLLGYN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   96 ACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINEttRWDEASFRTEVSYLEIYNERVRDLLrrkSSKTFNLRVR 175
Cdd:COG5059   91 CTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLED--LSMTKDFAVSISYLEIYNEKIYDLL---SPNEESLNIR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  176 EHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIkfTQAKFDSEMPCETVSKIHLVDLAG 255
Cdd:COG5059  166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI--ELASKNKVSGTSETSKLSLVDLAG 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  256 SERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlaKKKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATI 335
Cdd:COG5059  244 SERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----------KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTI 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  336 SPADVNYGETLSTLRYANRAKNIINKPTINEDANVKL--------IRELRAEIARLKTLLAQGNQIALLDSPTA--LSME 405
Cdd:COG5059  314 SPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReieeikfdLSEDRSEIEILVFREQSQLSQSSLSGIFAymQSLK 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  406 EKLQQNEARVQELTKEWTNKWNETQNILKEQTLALRKEG---------IGVVLDSELPHLIGIDDDLLSTGIILYHLKEG 476
Cdd:COG5059  394 KETETLKSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLqflrieidrLLLLREEELSKKKTKIHKLNKLRHDLSSLLSS 473

                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 41327691  477 QT-----YVGRDDASTEQDIVLHGLDLES--EHCIFENI 508
Cdd:COG5059  474 IPeetsdRVESEKASKLRSSASTKLNLRSsrSHSKFRDH 512
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
 446-562 1.53e-78

forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438784 [Multi-domain]  Cd Length: 117  Bit Score: 253.70  E-value: 1.53e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22732    1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGTVTLIPLNGAQCSVN 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 41327691  526 GVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22732   81 GVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
 1184-1311 3.53e-78

The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132784  Cd Length: 127  Bit Score: 253.07  E-value: 3.53e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691 1184 IKISIPRYVLCGQGKDAHFEFEVKITVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSH 1263
Cdd:cd06874    1 IKITIPRYVLRGQGKDEHFEFEVKITVLDETWTVFRRYSRFRELHKTMKLKYPEVAALEFPPKKLFGNKSERVAKERRRQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 41327691 1264 LEKYLRDFFSVMLQSATSPLHiNKVGLTLSKHTICEFSPFFKKGVFDY 1311
Cdd:cd06874   81 LETYLRNFFSVCLKLPACPLY-PKVGRTLSKATLCDFSPFFRKGVFEN 127
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 4-392 1.03e-73

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 269.88  E-value: 1.03e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691     4 VKVAVRVRPMNrreKDLEAKFIIQ-MEKSKTTITNlkipeggtgdsgrertKTFTYDfsfYSADTKSpdyvSQEMVFKTL 82
Cdd:PLN03188  100 VKVIVRMKPLN---KGEEGEMIVQkMSNDSLTING----------------QTFTFD---SIADPES----TQEDIFQLV 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGN---------SGDS-GLIPRICEGLFSRINE-----TTRwdEASFRTE 147
Cdd:PLN03188  154 GAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPanglleehlSGDQqGLTPRVFERLFARINEeqikhADR--QLKYQCR 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   148 VSYLEIYNERVRDLLRrKSSKtfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIF 227
Cdd:PLN03188  232 CSFLEIYNEQITDLLD-PSQK--NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVF 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   228 TIKFtqakfdsEMPCETV---------SKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADLSQDAan 298
Cdd:PLN03188  309 TCVV-------ESRCKSVadglssfktSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTG-- 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   299 tlakkKQVFVPYRDSVLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAKNIINKPTINE----DANV--KL 372
Cdd:PLN03188  380 -----KQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNFlrEV 454

                         410       420
                  ....*....|....*....|
gi 41327691   373 IRELRAEIARLKtllAQGNQ 392
Cdd:PLN03188  455 IRQLRDELQRVK---ANGNN 471
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 4-356 1.10e-72

Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276819 [Multi-domain]  Cd Length: 345  Bit Score: 246.54  E-value: 1.10e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    4 VKVAVRVRPMNRREKDLEAKFIIQMEKSkTTITnLKIPEGGTGDSGRERTKTFTYDFSFYSadTKSPDYvSQEMVFKTLG 83
Cdd:cd01368    3 VKVYLRVRPLSKDELESEDEGCIEVINS-TTVV-LHPPKGSAANKSERNGGQKETKFSFSK--VFGPNT-TQKEFFQGTA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   84 TDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFSRINETTRWdeasfrteVSYLEIYNERVRDLLR 163
Cdd:cd01368   78 LPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGGYSVF--------VSYIEIYNEYIYDLLE 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  164 RKSSKTF----NLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSE 239
Cdd:cd01368  150 PSPSSPTkkrqSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  240 MPCE------TVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaaNTLAKKKQVfVPYRDS 313
Cdd:cd01368  230 GDVDqdkdqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE------NQLQGTNKM-VPFRDS 302

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 41327691  314 VLTWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01368  303 KLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 3-356 5.18e-71

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 241.33  E-value: 5.18e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    3 SVKVAVRVRPMNRrekdlEAKFIIQMEKSKTTITNLKIPEGGTGDSGRERTK-TFTYDFSFYSAdtkspdyvSQEMVFKT 81
Cdd:cd01375    1 KVQAFVRVRPTDD-----FAHEMIKYGEDGKSISIHLKKDLRRGVVNNQQEDwSFKFDGVLHNA--------SQELVYET 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   82 LGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMG---NSGDSGLIPRICEGLFSRINEttRWDEAsFRTEVSYLEIYNERV 158
Cdd:cd01375   68 VAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGgteNYKHRGIIPRALQQVFRMIEE--RPTKA-YTVHVSYLEIYNEQL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  159 RDLL--RRKSSKTFN-LRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAK 235
Cdd:cd01375  145 YDLLstLPYVGPSVTpMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHS 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  236 FDSEMPCETVSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALADlsqdaantlakKKQVFVPYRDSVL 315
Cdd:cd01375  225 RTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD-----------KDRTHVPFRQSKL 293

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 41327691  316 TWLLKDSLGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01375  294 THVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 4-356 8.53e-68

Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276827 [Multi-domain]  Cd Length: 319  Bit Score: 231.62  E-value: 8.53e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTItnLKIPeggtgdsgRERTKTFTYDF-SFYSADTkspdyvSQEMVFKTL 82
Cdd:cd01376    2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVE--LADP--------RNHGETLKYQFdAFYGEES------TQEDIYARE 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   83 GTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEGLFsRINETTRWdeaSFRTEVSYLEIYNERVRDLL 162
Cdd:cd01376   66 VQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLL-QMTRKEAW---ALSFTMSYLEIYQEKILDLL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  163 RRKSSktfNLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTIKFTQAKFDSEMPC 242
Cdd:cd01376  142 EPASK---ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQ 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  243 ETvSKIHLVDLAGSERADATGATGVRLKEGGNINKSLVTLGNVISALadlsqdaantlaKKKQVFVPYRDSVLTWLLKDS 322
Cdd:cd01376  219 RT-GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL------------NKNLPRIPYRDSKLTRLLQDS 285

                        330       340       350
                 ....*....|....*....|....*....|....
gi 41327691  323 LGGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01376  286 LGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 4-356 3.63e-67

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276818 [Multi-domain]  Cd Length: 328  Bit Score: 229.88  E-value: 3.63e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    4 VKVAVRVRPMNRREKDLEAKFIIQMEKSKTTITNLkipeggtgdsgrERTK----------TFTYDFSFYSAdtkspdyV 73
Cdd:cd01367    2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHE------------PKLKvdltkyienhTFRFDYVFDES-------S 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   74 SQEMVFKTLGTDVVKSAFEGYNACVFAYGQTGSGKSYTMMGNSGDSGLIPRICEG----LFSRINETTRWDEasFRTEVS 149
Cdd:cd01367   63 SNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALaardVFRLLNKLPYKDN--LGVTVS 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  150 YLEIYNERVRDLLRRKSSktfnLRVREHPKEGPYVEDLSKHLVQNYGDVEELMDAGNINRTTAATGMNDVSSRSHAIFTI 229
Cdd:cd01367  141 FFEIYGGKVFDLLNRKKR----VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  230 KFTQAKFDsempcETVSKIHLVDLAGSER-ADATGATGVRLKEGGNINKSLVTLGNVISALAdlsqdaantlakKKQVFV 308
Cdd:cd01367  217 ILRDRGTN-----KLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALG------------QNKAHI 279

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 41327691  309 PYRDSVLTWLLKDSL-GGNSKTIMIATISPADVNYGETLSTLRYANRAK 356
Cdd:cd01367  280 PFRGSKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
 446-554 3.53e-65

forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 family includes StARD9/KIF16A and KIF16B. StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438760 [Multi-domain]  Cd Length: 109  Bit Score: 215.60  E-value: 3.53e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22708    1 GVVLDSELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGVVTLHPLPGALCAVN 80

                         90       100
                 ....*....|....*....|....*....
gi 41327691  526 GVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22708   81 GQVITQPTRLTQGDVILLGKTNMFRFNHP 109
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
 446-564 4.51e-49

forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438783 [Multi-domain]  Cd Length: 119  Bit Score: 169.96  E-value: 4.51e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  446 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVN 525
Cdd:cd22731    1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECGVVTLRPAQGAQCTVN 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 41327691  526 GVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLREKR 564
Cdd:cd22731   81 GREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQRR 119
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
 438-561 1.74e-34

forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 (PHLDB1) and similar proteins; PHLDB1, also called protein LL5-alpha (LL5A), acts as an insulin-responsive protein that enhances Akt activation. PHLDB1 contains a pleckstrin homology domain, which binds phosphatidylinositol PI(3,4)P(2), PI(3,5)P(2), and PI(3,4,5)P(3), as well as a Forkhead-associated (FHA) domain and coiled coil regions. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438765  Cd Length: 120  Bit Score: 128.21  E-value: 1.74e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  438 LALRKEGIGVVLDSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTeqdIVLHGLDLESEHCIFENIGGTVTLIPL 517
Cdd:cd22713    1 LELTETGKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDI---ISLQGPGVEPEHCYIENINGTVTLYPC 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 41327691  518 sGSQCSVNGVQIVEATHLNQGAVILLGRTNMFRFNHPKEAAKLR 561
Cdd:cd22713   78 -GNLCSVDGLPITEPTRLTQGCMICLGRSNYFRFNHPAEAKRMK 120
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
 453-553 6.58e-32

forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 family includes KIF1A, KIF1B, and KIF1C. KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438757 [Multi-domain]  Cd Length: 101  Bit Score: 120.03  E-value: 6.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  453 LPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQIVEA 532
Cdd:cd22705    1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDGVVTLEPCEGALTYVNGKRVTEP 80

                         90       100
                 ....*....|....*....|.
gi 41327691  533 THLNQGAVILLGRTNMFRFNH 553
Cdd:cd22705   81 TRLKTGSRVILGKNHVFRFNH 101
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
 1184-1305 3.36e-30

The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways.


Pssm-ID: 132810  Cd Length: 118  Bit Score: 115.91  E-value: 3.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691 1184 IKISIPRYVLCGQGKDAHFEFEVKITVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSH 1263
Cdd:cd07277    1 INVWIPSVFLRGKGSDAHHVYQVYIRIRDDEWNVYRRYSEFYELHKKLKKKFPVVRSFDFPPKKAIGNKDAKFVEERRKR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 41327691 1264 LEKYLRDFFSVMLQsaTSPlhinKVGLTLSKHTICEFSPFFK 1305
Cdd:cd07277   81 LQVYLRRVVNTLIQ--TSP----ELTACPSKETLIKLLPFFG 116
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
 450-554 7.60e-27

forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438759 [Multi-domain]  Cd Length: 108  Bit Score: 105.81  E-value: 7.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  450 DSELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQI 529
Cdd:cd22707    4 DNKLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGGKVTIIPVGDAETYVNGELI 83

                         90       100
                 ....*....|....*....|....*
gi 41327691  530 VEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22707   84 SEPTVLHHGDRVILGGDHYFRFNHP 108
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
 454-562 1.00e-25

forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438778 [Multi-domain]  Cd Length: 115  Bit Score: 103.08  E-value: 1.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGT-----VTLIPLSGSQCSVNGVQ 528
Cdd:cd22726    2 PHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSggeavVTLEPCEGADTYVNGKK 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 41327691  529 IVEATHLNQGAVILLGRTNMFRFNHPKEAAKLRE 562
Cdd:cd22726   82 VTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 115
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
 454-554 2.44e-25

forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438761 [Multi-domain]  Cd Length: 102  Bit Score: 101.52  E-value: 2.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLS-GSQCSVNGVQIVEA 532
Cdd:cd22709    1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNTDGKVTIEPVSpGAKVIVNGVPVTGE 80

                         90       100
                 ....*....|....*....|..
gi 41327691  533 THLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22709   81 TELHHLDRVILGSNHLYVFVGP 102
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
 454-556 3.64e-25

forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438779 [Multi-domain]  Cd Length: 110  Bit Score: 101.27  E-value: 3.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIF-----ENIGGTVTLIPLSGSQCSVNGVQ 528
Cdd:cd22727    3 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFrsernNNGEVIVTLEPCERSETYVNGKR 82

                         90       100
                 ....*....|....*....|....*...
gi 41327691  529 IVEATHLNQGAVILLGRTNMFRFNHPKE 556
Cdd:cd22727   83 VVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 6-288 1.01e-23

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 99.34  E-value: 1.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    6 VAVRVRPMNRREkdleakfIIQMEKSKTTitnlkipeggtgDSGRERtktftydfsfysadtkspdYVSQEMVFKTLGtD 85
Cdd:cd01363    1 VLVRVNPFKELP-------IYRDSKIIVF------------YRGFRR-------------------SESQPHVFAIAD-P 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   86 VVKSAFEGYN-ACVFAYGQTGSGKSYTMMgnsgdsGLIPRICEGLFSRIN--ETTRWDEASFRTevsyleiynervrdll 162
Cdd:cd01363   42 AYQSMLDGYNnQSIFAYGESGAGKTETMK------GVIPYLASVAFNGINkgETEGWVYLTEIT---------------- 99

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  163 rrkssktfnlrvrehpkegpyvedlskhlVQNYGDVEELMDAGNINRtTAATGMNDVSSRSHAIFTIkftqakfdsempc 242
Cdd:cd01363  100 -----------------------------VTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI------------- 136

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 41327691  243 etvskihLVDLAGSERadatgatgvrlkeggnINKSLVTLGNVISA 288
Cdd:cd01363  137 -------LLDIAGFEI----------------INESLNTLMNVLRA 159
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
 471-554 1.64e-20

forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 family includes KIF13A and KIF13B. KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438758 [Multi-domain]  Cd Length: 101  Bit Score: 87.73  E-value: 1.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  471 YHLKEgQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQCSVNGVQIVEATHLNQGAVILLGRTNMFR 550
Cdd:cd22706   19 YYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENEDVYLTPLEGARTCVNGSIVTEKTQLRHGDRILWGNNHFFR 97


                 ....
gi 41327691  551 FNHP 554
Cdd:cd22706   98 LNCP 101
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 1185-1273 1.01e-19

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


Pssm-ID: 132768 [Multi-domain]  Cd Length: 106  Bit Score: 85.49  E-value: 1.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691 1185 KISIPRYVLCGQGKDAHFEFEVKITVLD-ETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSH 1263
Cdd:cd06093    1 SVSIPDYEKVKDGGKKYVVYIIEVTTQGgEEWTVYRRYSDFEELHEKLKKKFPGVILPPLPPKKLFGNLDPEFIEERRKQ 80

                         90
                 ....*....|
gi 41327691 1264 LEKYLRDFFS 1273
Cdd:cd06093   81 LEQYLQSLLN 90
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
 454-553 2.21e-18

forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438780 [Multi-domain]  Cd Length: 102  Bit Score: 81.46  E-value: 2.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  454 PHLIGIDDDLLSTGIILYHLKEGQTYVGRDDAsteqDIVLHGLDLESEHCIFENIGG-----TVTLIPLSGSQCSVNGVQ 528
Cdd:cd22728    2 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLSGQFIREQHCLFRSIPNpsgevVVTLEPCEGAETYVNGKQ 77

                         90       100
                 ....*....|....*....|....*
gi 41327691  529 IVEATHLNQGAVILLGRTNMFRFNH 553
Cdd:cd22728   78 VTEPLVLKSGNRIVMGKNHVFRFNH 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 595-1078 7.72e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 83.06  E-value: 7.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  595 GLEFERQQREELE-KLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLL 673
Cdd:COG1196  303 DIARLEERRRELEeRLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  674 AEKEKFEEERLReqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEE 753
Cdd:COG1196  383 ELAEELLEALRA-----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  754 QEKEQVMLVAHLEEQLREKQEMIQLLR-RGEVQWVEEEKRDLEGIRESLLR-VKEARAGGDEDGEELEKAQLRFFEFKRR 831
Cdd:COG1196  458 EEALLELLAELLEEAALLEAALAELLEeLAEAAARLLLLLEAEADYEGFLEgVKAALLLAGLRGLAGAVAVLIGVEAAYE 537

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  832 QLV----------KLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDfekikPVEYR 901
Cdd:COG1196  538 AALeaalaaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD-----LREAD 612

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  902 LQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLdnTLYQVEKEMEEKEEQLAQYQANANQLQKLQATfeftANIAR 981
Cdd:COG1196  613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV--TLEGEGGSAGGSLTGGSRRELLAALLEAEAEL----EELAE 686

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  982 QEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLAslnsgsrEQSGLQASLEAEQEALE 1061
Cdd:COG1196  687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL-------EEEELLEEEALEELPEP 759

                        490
                 ....*....|....*..
gi 41327691 1062 KDQERLEYEIQQLKQKI 1078
Cdd:COG1196  760 PDLEELERELERLEREI 776
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
 453-554 5.83e-15

forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ALL1-fused gene from chromosome 6 protein, protein AF-6, Afadin adherens junction formation factor, or MLLT4, is a nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. It is essential for the organization of adherens junctions. It may play a key role in the organization of epithelial structures of the embryonic ectoderm. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438763 [Multi-domain]  Cd Length: 106  Bit Score: 71.97  E-value: 5.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  453 LPHLI-----GIDDDLLstgiILYHLKEGQTYVG--RDDASTEQDIVLHGLDLESEHCIFENIGGTVTLIPLSG-SQCSV 524
Cdd:cd22711    1 LPYLLelspdGSDRDKP----RRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHMEGVVTVTPASQdAETYV 76

                         90       100       110
                 ....*....|....*....|....*....|
gi 41327691  525 NGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22711   77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 600-1077 7.85e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 79.98  E-value: 7.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  600 RQQREELEKLESKRKL--IEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLlaeke 677
Cdd:COG1196  216 RELKEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE----- 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  678 kfeeerlreqqeielqkkRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKE 757
Cdd:COG1196  291 ------------------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  758 QVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESL-LRVKEARAGGDEDGEELEKAQLRffEFKRRQLVKL 836
Cdd:COG1196  353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAeLAAQLEELEEAEEALLERLERLE--EELEELEEAL 430

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  837 VNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNH 916
Cdd:COG1196  431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  917 LPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQ---------LAQYQANANQLQKLQATFEFTANIARQEEKVR 987
Cdd:COG1196  511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnivveddevAAAAIEYLKAAKAGRATFLPLDKIRARAALAA 590

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  988 KKEKEI--------------LESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASL 1053
Cdd:COG1196  591 ALARGAigaavdlvasdlreADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670

                        490       500
                 ....*....|....*....|....
gi 41327691 1054 EAEQEALEKDQERLEYEIQQLKQK 1077
Cdd:COG1196  671 LAALLEAEAELEELAERLAEEELE 694
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 3-162 9.72e-15

Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 72.64  E-value: 9.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691      3 SVKVAVRVRPMNRREkdleakfiIQMEKSKTTITNLKIpeggtgdsgRERTKTFTYDFSFYSADTkspdyvsQEMVFKTL 82
Cdd:pfam16796   21 NIRVFARVRPELLSE--------AQIDYPDETSSDGKI---------GSKNKSFSFDRVFPPESE-------QEDVFQEI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691     83 GTdVVKSAFEGYNACVFAYGQTGSGksytmmgnsGDSGLIPRICEGLFSRINETTRwdEASFRTEVSYLEIYNERVRDLL 162
Cdd:pfam16796   77 SQ-LVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKK--GWKYTIELQFVEIYNESSQDLL 144
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
 1181-1268 5.51e-13

The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor Antisera-Selected; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Imidazoline Receptor Antisera-Selected (IRAS), also called nischarin, contains an N-terminal PX domain, leucine rich repeats, and a predicted coiled coil domain. The PX domain of IRAS binds to phosphatidylinositol-3-phosphate in membranes. Together with the coiled coil domain, it is essential for the localization of IRAS to endosomes. IRAS has been shown to interact with integrin and inhibit cell migration. Its interaction with alpha5 integrin causes a redistribution of the receptor from the cell surface to endosomal structures, suggesting that IRAS may function as a sorting nexin (SNX) which regulates the endosomal trafficking of integrin. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132785  Cd Length: 116  Bit Score: 66.53  E-value: 5.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691 1181 KDPIKISIPRYVLcgqgKDAHFEFEVKITVLDETWTVFRRYSRFREMHKTLKLKYAELAALeFPPKKLFGNKDERVIAER 1260
Cdd:cd06875    1 EPETKIRIPSAET----VEGYTVYIIEVKVGSVEWTVKHRYSDFAELHDKLVAEHKVDKDL-LPPKKLIGNKSPSFVEKR 75


                 ....*...
gi 41327691 1261 RSHLEKYL 1268
Cdd:cd06875   76 RKELEIYL 83
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 592-926 8.69e-13

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: 72.85  E-value: 8.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    592 YNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEivqlQIRKQEESLKRRSFHIEnKLKD 671
Cdd:pfam17380  260 YNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKARQAEMD-RQAA 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    672 LLAEKEKFEEERLREQQEIELQKKRQEEETfLRVQE---ELQRLKELnnnekaekfqifqELDQLQKEKDEQYAKLELEK 748
Cdd:pfam17380  335 IYAEQERMAMERERELERIRQEERKRELER-IRQEEiamEISRMREL-------------ERLQMERQQKNERVRQELEA 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    749 KR----LEEQEKEQVMLVAHLEEQLREKQEMIqllRRGEVQWVEEEK-RDLEGIRESLLRVKEARAGGDEDGEELEKAQL 823
Cdd:pfam17380  401 ARkvkiLEEERQRKIQQQKVEMEQIRAEQEEA---RQREVRRLEEERaREMERVRLEEQERQQQVERLRQQEEERKRKKL 477

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    824 RFFEFKRRQlvklvnlEKDLVQQKDILKKEVQEEQEILeclkCEHDKESRLLEKHDESVTdvTEVPQDFEKIKPVEYRLQ 903
Cdd:pfam17380  478 ELEKEKRDR-------KRAEEQRRKILEKELEERKQAM----IEEERKRKLLEKEMEERQ--KAIYEEERRREAEEERRK 544

                          330       340
                   ....*....|....*....|...
gi 41327691    904 YKERQLQYLLQNHLPTLLEEKQR 926
Cdd:pfam17380  545 QQEMEERRRIQEQMRKATEERSR 567
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
 456-564 1.13e-12

forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438781 [Multi-domain]  Cd Length: 109  Bit Score: 65.68  E-value: 1.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  456 LIGIDDDLLSTGIILYHLKeGQTYVGRDdasTEQDIVLHGLDLESEHCIFE-NIGGTVTLIPLSGSQCSVNGVQIVEATH 534
Cdd:cd22729    4 LVNLNADPALNELLVYYLK-DHTRVGAD---TSQDIQLFGIGIQPEHCVIDiAADGDVTLTPKENARTCVNGTLVCSVTQ 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 41327691  535 LNQGAVILLGRTNMFRFNHPKEAAKLREKR 564
Cdd:cd22729   80 LWHGDRILWGNNHFFRINLPKRKRRDWLKE 109
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
 1212-1268 2.06e-12

The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX13, also called RGS-PX1, contains an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. It specifically binds to the stimulatory subunit of the heterotrimeric G protein G(alpha)s, serving as its GTPase activating protein, through the RGS domain. It preferentially binds phosphatidylinositol-3-phosphate (PI3P) through the PX domain and is localized in early endosomes. SNX13 is involved in endosomal sorting of EGFR into multivesicular bodies (MVB) for delivery to the lysosome.


Pssm-ID: 132783  Cd Length: 120  Bit Score: 65.37  E-value: 2.06e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41327691 1212 DETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYL 1268
Cdd:cd06873   38 EESWHVYRRYSDFHDLHMRLKEKFPNLSKLSFPGKKTFNNLDRAFLEKRRKMLNQYL 94
PX_MONaKA cd06871
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ...
 1196-1268 3.46e-12

The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. MONaKA (Modulator of Na,K-ATPase) binds the plasma membrane ion transporter, Na,K-ATPase, and modulates its enzymatic and ion pump activities. It modulates brain Na,K-ATPase and may be involved in regulating electrical excitability and synaptic transmission. MONaKA contains an N-terminal PX domain and a C-terminal catalytic kinase domain. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.


Pssm-ID: 132781  Cd Length: 120  Bit Score: 64.69  E-value: 3.46e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41327691 1196 QGKDAHFEFEVKIT--VLDE-TWTVFRRYSRFREMHKTLKLKYAELAaleFPPKKLFGNKDERVIAERRSHLEKYL 1268
Cdd:cd06871   16 QNIQSHTEYIIRVQrgPSPEnSWQVIRRYNDFDLLNASLQISGISLP---LPPKKLIGNMDREFIAERQQGLQNYL 88
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 1212-1269 5.37e-12

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 62.64  E-value: 5.37e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 41327691   1212 DETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYLR 1269
Cdd:pfam00787    6 LEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRYNEEFIEKRRKGLEQYLQ 63
PTZ00121 PTZ00121
MAEBL; Provisional
 599-859 1.37e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 69.78  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   599 ERQQREELEKLESKRKLIE--EMEEKQKSD---KAELERMQQE---VETQRKETEIVQLQIRKQEESLKRRSFHIENKLK 670
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEakKAEEKKKADelkKAEELKKAEEkkkAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   671 dLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQyaKLELEKKR 750
Cdd:PTZ00121 1600 -LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK--KAEEDKKK 1676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   751 LEEQEKEQVMLVAHLEEQLREKQEM--IQLLRRGEvqwvEEEKRDLEGIR----ESLLRVKEARAGGDEDGEELEKAQLR 824
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAkkAEELKKKE----AEEKKKAEELKkaeeENKIKAEEAKKEAEEDKKKAEEAKKD 1752

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 41327691   825 FFEFKRRQLVKLVNLEKDLVQQKD---ILKKEVQEEQE 859
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEkeaVIEEELDEEDE 1790
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 1197-1269 1.67e-11

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 61.98  E-value: 1.67e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41327691    1197 GKDAHFEFEVKITVLDETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFG---NKDERVIAERRSHLEKYLR 1269
Cdd:smart00312   10 GKHYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGrlnNFSEEFIEKRRRGLEKYLQ 85
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 597-894 3.06e-11

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: 68.16  E-value: 3.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    597 EFERQQREELEKLESKRKLIEEMEEkqksdkaELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLAEK 676
Cdd:TIGR02168  257 ELTAELQELEEKLEELRLEVSELEE-------EIEELQKELYALANEISRLEQQKQILRERLAN----LERQLEELEAQL 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    677 EKFEEERLREQQEIELQKKRQEEetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 756
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEE-----LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    757 EQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKL 836
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 41327691    837 VNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRlLEKHDESVTDVTEVPQDFEK 894
Cdd:TIGR02168  481 ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG-LSGILGVLSELISVDEGYEA 537
Kinesin_assoc pfam16183
Kinesin-associated;
364-476 3.07e-11

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 63.71  E-value: 3.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    364 INEDANVKLIRELRAEIARLKTLL-AQG----------------NQIA-------------------------------- 394
Cdd:pfam16183    3 INEDPNNKLIRELKDEVARLRDLLyAQGlgdiidtiahptkkraNTPAanasaataamagaspspslsalssraasvssl 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    395 ---LLDSPTALSMEEKLQQNEARVQELTKEWTNKWNETQNI-------LKEQTLALRKEG--IGVVLDSELPHLIGIDDD 462
Cdd:pfam16183   83 herIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIrmerealLAEMGVAIREDGgtLGVFSPKKTPHLVNLNED 162

                          170
                   ....*....|....
gi 41327691    463 LLSTGIILYHLKEG 476
Cdd:pfam16183  163 PLMSECLLYYIKDG 176
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
 456-554 4.92e-11

forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438782 [Multi-domain]  Cd Length: 99  Bit Score: 60.70  E-value: 4.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  456 LIGIDDDLLSTGIILYHLKEgQTYVGRDDAsteQDIVLHGLDLESEHCIFE-NIGGTVTLIPLSGSQCSVNGVQIVEATH 534
Cdd:cd22730    4 LVNLNADPALNELLVYYLKE-HTLIGSADS---QDIQLCGMGILPEHCIIDiTPEGQVMLTPQKNTRTFVNGSAVTSPIQ 79

                         90       100
                 ....*....|....*....|
gi 41327691  535 LNQGAVILLGRTNMFRFNHP 554
Cdd:cd22730   80 LHHGDRILWGNNHFFRINLP 99
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 599-1019 7.53e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 7.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  599 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 678
Cdd:COG1196  339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  679 FEEERLREQQEIE--LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 756
Cdd:COG1196  419 LEEELEELEEALAelEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  757 EQVMLVAHLEEQLREKQEMIQLLRRGEVQ---WVEEEKRDLEGIRESLLRVKEARAggDEDGEELEKAQLRFFEFKRRQL 833
Cdd:COG1196  499 AEADYEGFLEGVKAALLLAGLRGLAGAVAvliGVEAAYEAALEAALAAALQNIVVE--DDEVAAAAIEYLKAAKAGRATF 576

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  834 VKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVP-QDFEKIKPVEYRLQYKERQLQYL 912
Cdd:COG1196  577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLeAALRRAVTLAGRLREVTLEGEGG 656

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  913 LQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKE 992
Cdd:COG1196  657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 41327691  993 ILESREKQQ----------------REALERALARLERRHSAL 1019
Cdd:COG1196  737 LLEELLEEEelleeealeelpeppdLEELERELERLEREIEAL 779
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 602-933 2.01e-10

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: 65.47  E-value: 2.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    602 QREELEKLESKRKLIEEMeekqksdKAELERMQQEVEtqRKETEIVQLQIRKQEESlkRRSFHIENKLKDLLAEKEKFEE 681
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGL-------KRELSSLQSELR--RIENRLDELSQELSDAS--RKIGEIEKEIEQLEQEEEKLKE 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    682 ERLREQQEI-ELQKKRQEEETFL-RVQEELQRLKELNNNEKAEKFQIFQELDQLQ-KEKDEQYAKLELEKKRLEE--QEK 756
Cdd:TIGR02169  738 RLEELEEDLsSLEQEIENVKSELkELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEArlREI 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    757 EQVMLVAHLEEQLREK--QEMIQLLRRGEVQWVEEEKR--DLEGIRESLL-RVKEARAGGDEDGEELE---------KAQ 822
Cdd:TIGR02169  818 EQKLNRLTLEKEYLEKeiQELQEQRIDLKEQIKSIEKEieNLNGKKEELEeELEELEAALRDLESRLGdlkkerdelEAQ 897

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    823 LRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRL 902
Cdd:TIGR02169  898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLA 977

                          330       340       350
                   ....*....|....*....|....*....|....
gi 41327691    903 --QYKERQLQYL-LQNHLPTLLEEKQrafEILDR 933
Cdd:TIGR02169  978 iqEYEEVLKRLDeLKEKRAKLEEERK---AILER 1008
PTZ00121 PTZ00121
MAEBL; Provisional
 555-813 2.81e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.16  E-value: 2.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   555 KEAAKLREKRKSGLLSSFSLSMTDLSKSRENLSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEeKQKSDKAELERMQ 634
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-KAEEEKKKVEQLK 1639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   635 QEVETQRKETEivqlQIRKQEESLKRRSFHIENKlkdllAEKEKfeeeRLREQQEIELQKKRQEEETFLRVQEELQRLKE 714
Cdd:PTZ00121 1640 KKEAEEKKKAE----ELKKAEEENKIKAAEEAKK-----AEEDK----KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   715 LNNNEKAEKfqifQELDQLQKEKDEQYAKLELEKKRLEEQEKEqvmlVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDL 794
Cdd:PTZ00121 1707 LKKKEAEEK----KKAEELKKAEEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778

                         250
                  ....*....|....*....
gi 41327691   795 EGIRESLLRVKEARAGGDE 813
Cdd:PTZ00121 1779 AVIEEELDEEDEKRRMEVD 1797
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
 1185-1270 4.85e-10

The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of fungal proteins similar to Saccharomyces cerevisiae Vam7p. They contain an N-terminal PX domain and a C-terminal SNARE domain. The SNARE (Soluble NSF attachment protein receptor) family of proteins are integral membrane proteins that serve as key factors for vesicular trafficking. Vam7p is anchored at the vacuolar membrane through the specific interaction of its PX domain with phosphatidylinositol-3-phosphate (PI3P) present in bilayers. It plays an essential role in vacuole fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132807  Cd Length: 108  Bit Score: 58.05  E-value: 4.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691 1185 KISIPRYVLcgQGKDAHFeFEVKITVLDETWTVFRRYSRFREMHKTL-KLKYAELAAlEFPPKKLF--GNKDERVIAERR 1261
Cdd:cd06897    2 EISIPTTSV--SPKPYTV-YNIQVRLPLRSYTVSRRYSEFVALHKQLeSEVGIEPPY-PLPPKSWFlsTSSNPKLVEERR 77


                 ....*....
gi 41327691 1262 SHLEKYLRD 1270
Cdd:cd06897   78 VGLEAFLRA 86
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 455-551 9.35e-10

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 56.51  E-value: 9.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  455 HLIGIDDDllsTGIILYHLKEGQTYVGRDDASteqDIVLHGLDLESEHCIFENIGGTVTLIPLSGSQ-CSVNGVQIVEAT 533
Cdd:cd00060    1 RLIVLDGD---GGGREFPLTKGVVTIGRSPDC---DIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNgTFVNGKRITPPV 74

                         90
                 ....*....|....*...
gi 41327691  534 HLNQGAVILLGRTNmFRF 551
Cdd:cd00060   75 PLQDGDVIRLGDTT-FRF 91
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 603-1136 1.32e-09

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: 62.78  E-value: 1.32e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    603 REELEKLESKrklIEEMEEKQKSDKAELERMQQEVE-TQRKETEIVQLQIRKQEESLKRRS--FHIENKLKDLLAEKEKF 679
Cdd:TIGR02169  363 KEELEDLRAE---LEEVDKEFAETRDELKDYREKLEkLKREINELKRELDRLQEELQRLSEelADLNAAIAGIEAKINEL 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    680 EEERLREQQEIELQkkrqeeetflrvQEELQRLKELNNNEKAEKFQIFQELDQLQKE---KDEQYAKLELEKKRLEEQEK 756
Cdd:TIGR02169  440 EEEKEDKALEIKKQ------------EWKLEQLAADLSKYEQELYDLKEEYDRVEKElskLQRELAEAEAQARASEERVR 507

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    757 EQVMLVAHLEEQLREKQEMIQLLRRGEVQW----------------VEEEK---------RDLEGIRESLLRVKEARAGG 811
Cdd:TIGR02169  508 GGRAVEEVLKASIQGVHGTVAQLGSVGERYataievaagnrlnnvvVEDDAvakeaiellKRRKAGRATFLPLNKMRDER 587

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    812 DEDGEELEKAQLRF---------------------------FEFKRRQL--VKLVNLEKDLVQQ---------------- 846
Cdd:TIGR02169  588 RDLSILSEDGVIGFavdlvefdpkyepafkyvfgdtlvvedIEAARRLMgkYRMVTLEGELFEKsgamtggsraprggil 667

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    847 -KDILKKEVQEEQEILECLKCEhdkESRLLEKHDESVTDVTEVpqdFEKIKPVEYRLQYKERQLQYLLQNH--LPTLLEE 923
Cdd:TIGR02169  668 fSRSEPAELQRLRERLEGLKRE---LSSLQSELRRIENRLDEL---SQELSDASRKIGEIEKEIEQLEQEEekLKERLEE 741

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    924 KQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQL---------QKLQATFEFTANIARQEEKVRKKEKEIL 994
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshsriPEIQAELSKLEEEVSRIEARLREIEQKL 821

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    995 ESREkQQREALERALARLERRHSALQ-RHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQ 1073
Cdd:TIGR02169  822 NRLT-LEKEYLEKEIQELQEQRIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41327691   1074 LKQKIYEV----------DGVQKDHHGTLEGKVASSSLPVSAEKSHLVPLMDARINAYIEEEVQRRLQDLHRV 1136
Cdd:TIGR02169  901 LERKIEELeaqiekkrkrLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPV 973
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 601-861 1.50e-09

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: 62.77  E-value: 1.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    601 QQREELEKLESKRKLIE----EMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLlaEK 676
Cdd:TIGR02168  674 ERRREIEELEEKIEELEekiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI--AQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    677 EKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQ---YAKLELEKKRLEE 753
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeAANLRERLESLER 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    754 QEKEQVMLVAHLEEQLREKQEMIQLL---RRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEkAQLRFFEFK- 829
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALLNERASLEEALALLRSELEELS-EELRELESKr 910

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 41327691    830 ---RRQLVKLVNLEKDLVQQKDILKKEVQEEQEIL 861
Cdd:TIGR02168  911 selRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 600-1078 1.68e-09

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: 62.77  E-value: 1.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    600 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKF 679
Cdd:TIGR02168  305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    680 EEERLREQQEIELQKKRQEeetflRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEK-DEQYAKLELEKKRLEEQEKEQ 758
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIE-----RLEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEELERL 459

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    759 VMLVAHLEEQLREKQEMIQLLRRGEVQwveeekrdLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRqLVKLVN 838
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQ--------LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV-LSELIS 530

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    839 LEK------DLVQQKDILKKEVQEEQEILECLkcEHDKESRL---------LEKHDESVTDVTEVPQDFEKIKPVEYRLQ 903
Cdd:TIGR02168  531 VDEgyeaaiEAALGGRLQAVVVENLNAAKKAI--AFLKQNELgrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLV 608

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    904 YKERQLQYLLQNHLPTLL--EEKQRAFEILDR-----------------------GPLSLDNTLYQVEKEMEEKEEQLAQ 958
Cdd:TIGR02168  609 KFDPKLRKALSYLLGGVLvvDDLDNALELAKKlrpgyrivtldgdlvrpggvitgGSAKTNSSILERRREIEELEEKIEE 688

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    959 YQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERrhsALQRHSTLGMEIEEQRQKLAS 1038
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ---LEERIAQLSKELTELEAEIEE 765

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 41327691   1039 LNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKI 1078
Cdd:TIGR02168  766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 595-935 2.45e-09

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: 61.91  E-value: 2.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    595 GLEFERQQREELEKLESK-----RKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKL 669
Cdd:pfam02463  164 GSRLKRKKKEALKKLIEEtenlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    670 KDLLAEKEKFEEErlreQQEIELQKKRQEEETFL-----RVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKL 744
Cdd:pfam02463  244 ELLRDEQEEIESS----KQEIEKEEEKLAQVLKEnkeeeKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    745 ELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLR 824
Cdd:pfam02463  320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    825 FFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQY 904
Cdd:pfam02463  400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479

                          330       340       350
                   ....*....|....*....|....*....|.
gi 41327691    905 KERQLQYLLQNHLPTLLEEKQRAFEILDRGP 935
Cdd:pfam02463  480 VKLQEQLELLLSRQKLEERSQKESKARSGLK 510
PTZ00121 PTZ00121
MAEBL; Provisional
 536-1153 3.67e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.70  E-value: 3.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   536 NQGAVILLGRTNMFRFNHPKEAAKLREKRKSGL--LSSFSLSMTDLSKSRENLSAvmlynpglEFERQQREELEKLESKR 613
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADElkKAEEKKKADEAKKAEEKKKA--------DEAKKKAEEAKKADEAK 1321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   614 KLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEERLREQQEIELQ 693
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   694 KKRQEEETFLRVQEELQRLKELnnNEKAEKFQIFQELdqlqKEKDEQYAKLELEKKRLEEQEKEQvmlvaHLEEQLREKQ 773
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEA--KKKAEEKKKADEA----KKKAEEAKKADEAKKKAEEAKKAE-----EAKKKAEEAK 1470

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   774 EMIQLLRRG-EVQWVEEEKRDLEGIR---ESLLRVKEARAGGDE--DGEELEKA-QLRFFEFKRrqlvKLVNLEK-DLVQ 845
Cdd:PTZ00121 1471 KADEAKKKAeEAKKADEAKKKAEEAKkkaDEAKKAAEAKKKADEakKAEEAKKAdEAKKAEEAK----KADEAKKaEEKK 1546

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   846 QKDILKK--EVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQyllqnhlpTLLEE 923
Cdd:PTZ00121 1547 KADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--------KAEEA 1618

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   924 KQRAFEIldrgplsldNTLYQVEKEMEEKEEQLAQYQANANQLQKlqatfeftaniARQEEKVRKKEKEILESREKQQRE 1003
Cdd:PTZ00121 1619 KIKAEEL---------KKAEEEKKKVEQLKKKEAEEKKKAEELKK-----------AEEENKIKAAEEAKKAEEDKKKAE 1678

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  1004 ALERALARLERRHSALQRHstlgmeiEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDG 1083
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKE-------AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  1084 VQKDhhgtlEGKVASSSLPVSAEKSHLVPLMDARINAYIEEEVQRRLQDLHRVISEGCSTSADTMKDNEK 1153
Cdd:PTZ00121 1752 DEEE-----KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
587-1080 3.87e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 60.94  E-value: 3.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  587 SAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIE 666
Cdd:COG4717   54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  667 -NKLKDLLAEKEKfeeerlreqqeiELQKKRQEEETFLRVQEELQRLKElnnNEKAEKFQIFQELDQLQKEKDEQYAKLE 745
Cdd:COG4717  134 lEALEAELAELPE------------RLEELEERLEELRELEEELEELEA---ELAELQEELEELLEQLSLATEEELQDLA 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  746 LEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIresLLRVKEARAGGDEDGEELEKAQLRF 825
Cdd:COG4717  199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL---LLLIAAALLALLGLGGSLLSLILTI 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  826 FEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKH----DESVTDVTEVPQDFEKIKPVEYR 901
Cdd:COG4717  276 AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppDLSPEELLELLDRIEELQELLRE 355

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  902 LQYKERQLQyllqnhlptLLEEKQRAFEILDRGPLSLDNTLYQvekemeeKEEQLAQYQANANQLQKLQATFEftaniar 981
Cdd:COG4717  356 AEELEEELQ---------LEELEQEIAALLAEAGVEDEEELRA-------ALEQAEEYQELKEELEELEEQLE------- 412

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  982 qeekvrKKEKEILESREKQQREALERALARLERRHSALQRhstlgmEIEEQRQKLaslnsgsreqsglqASLEAEQEALE 1061
Cdd:COG4717  413 ------ELLGELEELLEALDEEELEEELEELEEELEELEE------ELEELREEL--------------AELEAELEQLE 466

                        490       500
                 ....*....|....*....|.
gi 41327691 1062 KDQE--RLEYEIQQLKQKIYE 1080
Cdd:COG4717  467 EDGElaELLQELEELKAELRE 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 600-916 5.97e-09

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: 60.84  E-value: 5.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    600 RQQREELE-KLESKRK-------LIEEMEEKQKSDKAELERMQ--QEVETQRKETEIVQLQIRKQEESLKRRSFhiENKL 669
Cdd:TIGR02168  171 KERRKETErKLERTREnldrledILNELERQLKSLERQAEKAEryKELKAELRELELALLVLRLEELREELEEL--QEEL 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    670 KDLLAEKEKFEEERLREQQEI-ELQKKRQE-EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELE 747
Cdd:TIGR02168  249 KEAEEELEELTAELQELEEKLeELRLEVSElEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    748 KKRLEEQEKEQVML----------VAHLEEQLREKQEMIQLLRRGEVQW---VEEEKRDLEGIRESLLRVKEARAGGDED 814
Cdd:TIGR02168  329 ESKLDELAEELAELeekleelkeeLESLEAELEELEAELEELESRLEELeeqLETLRSKVAQLELQIASLNNEIERLEAR 408

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    815 GEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQkdilkkEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEK 894
Cdd:TIGR02168  409 LERLEDRRERLQQEIEELLKKLEEAELKELQA------ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482

                          330       340
                   ....*....|....*....|..
gi 41327691    895 ikpVEYRLQYKERQLQYLLQNH 916
Cdd:TIGR02168  483 ---ELAQLQARLDSLERLQENL 501
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 586-809 1.24e-08

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: 58.62  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  586 LSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhI 665
Cdd:COG4942    6 LLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA----L 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  666 ENKLKDLLAEKEKFEEERLREQQEIE-----LQKKRQEE--------ETFLRVQEELQRLKELNNNEKAEKFQIFQELDQ 732
Cdd:COG4942   82 EAELAELEKEIAELRAELEAQKEELAellraLYRLGRQPplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  733 L----------QKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgevqwveeEKRDLEGIRESLL 802
Cdd:COG4942  162 LaalraeleaeRAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ--------EAEELEALIARLE 233


                 ....*..
gi 41327691  803 RVKEARA 809
Cdd:COG4942  234 AEAAAAA 240
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 596-774 1.72e-08

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: 58.81  E-value: 1.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    596 LEFERQQREEleklESKRKLIEEMEEKQKSDKAELERMQQevetqrKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAE 675
Cdd:pfam15709  348 LEVERKRREQ----EEQRRLQQEQLERAEKMREELELEQQ------RRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAA 417

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    676 KEKFEEERLREQQEI-ELQKKRQEEETfLRVQEELQRLKELnNNEKAEKFQIFQELD-------QLQKEKDEQYAKLELE 747
Cdd:pfam15709  418 QERARQQQEEFRRKLqELQRKKQQEEA-ERAEAEKQRQKEL-EMQLAEEQKRLMEMAeeerleyQRQKQEAEEKARLEAE 495

                          170       180
                   ....*....|....*....|....*..
gi 41327691    748 KKRleEQEKEQVMLVahLEEQLREKQE 774
Cdd:pfam15709  496 ERR--QKEEEAARLA--LEEAMKQAQE 518
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
600-1068 2.43e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.54  E-value: 2.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   600 RQQREELEKLESKRKLIEEMEEKQKS----------DKAELERMQQEVETQRKETEIVQLQIrKQEESLKRRSFHIENKL 669
Cdd:PRK03918  269 EELKKEIEELEEKVKELKELKEKAEEyiklsefyeeYLDELREIEKRLSRLEEEINGIEERI-KELEEKEERLEELKKKL 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   670 KDLLAEKEkfeeerlreqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKfqIFQELDQLQKEKDEQYAKLELEKK 749
Cdd:PRK03918  348 KELEKRLE-------------ELEERHELYEEAKAKKEELERLKKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITA 412

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   750 RLEEQEKEQVMLVAHLEEqLREKQEMIQLLRRgevQWVEEEKRDLegIRESLLRVKEARAGGDEDGEELEKAQLRFfefk 829
Cdd:PRK03918  413 RIGELKKEIKELKKAIEE-LKKAKGKCPVCGR---ELTEEHRKEL--LEEYTAELKRIEKELKEIEEKERKLRKEL---- 482

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   830 rRQLVKLVNLEKDLVQQKDILK--KEVQEEQEILECLKCEHDKE--SRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYK 905
Cdd:PRK03918  483 -RELEKVLKKESELIKLKELAEqlKELEEKLKKYNLEELEKKAEeyEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL 561

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   906 ERQLQYL---LQNHLPTLLEEKQRAFEILDRGPLSLDnTLYQVEKEMEEKEEQLaqyQANANQLQKLQATFEFT-ANIAR 981
Cdd:PRK03918  562 EKKLDELeeeLAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKEL---EREEKELKKLEEELDKAfEELAE 637

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   982 QEEKVRKKEKEILESREK---QQREALERALARLERRHSALQRHSTlgmEIEEQRQKLASLNSGSREQSGLQASLEAEQE 1058
Cdd:PRK03918  638 TEKRLEELRKELEELEKKyseEEYEELREEYLELSRELAGLRAELE---ELEKRREEIKKTLEKLKEELEEREKAKKELE 714

                         490
                  ....*....|
gi 41327691  1059 ALEKDQERLE 1068
Cdd:PRK03918  715 KLEKALERVE 724
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 555-1077 2.74e-08

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: 58.44  E-value: 2.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    555 KEAAKLREKRKSGLLSSFSLSMTDLSKSRENLSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAE-LERM 633
Cdd:pfam02463  275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIkREAE 354

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    634 QQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRlk 713
Cdd:pfam02463  355 EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL-- 432

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    714 elnnnEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRD 793
Cdd:pfam02463  433 -----EEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    794 LEGIRESLLRVKEARAGGDEDGeELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEI---LECLKCEHDK 870
Cdd:pfam02463  508 GLKVLLALIKDGVGGRIISAHG-RLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELplgARKLRLLIPK 586

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    871 ESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNTLyQVEKEME 950
Cdd:pfam02463  587 LKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGL-AEKSEVK 665

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    951 EKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLgmEIE 1030
Cdd:pfam02463  666 ASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKL--LKQ 743

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*..
gi 41327691   1031 EQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQK 1077
Cdd:pfam02463  744 KIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE 790
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 695-1068 3.64e-08

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: 58.16  E-value: 3.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    695 KRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAK---LELEKKRLEEQEKEQVMLVAHLEEQLRE 771
Cdd:TIGR02169  669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeIEKEIEQLEQEEEKLKERLEELEEDLSS 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    772 KQEMIQLLRRgEVQWVEEEKRDLEgirESLLRVKEARAG--GDEDGEELEK--AQLRFFEFKRRQLVKLVN-LEKDL--- 843
Cdd:TIGR02169  749 LEQEIENVKS-ELKELEARIEELE---EDLHKLEEALNDleARLSHSRIPEiqAELSKLEEEVSRIEARLReIEQKLnrl 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    844 VQQKDILKKEVQEEQEILECLKcehDKESRLLEKHDESVTDVtevpqdfEKIKPVEYRLQYKERQLQYLLQNhlptllee 923
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLK---EQIKSIEKEIENLNGKK-------EELEEELEELEAALRDLESRLGD-------- 886

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    924 kqrafeiLDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQ-KLQATFEFTANIARQEEKVRKKEKEILESRE-KQQ 1001
Cdd:TIGR02169  887 -------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKaKLEALEEELSEIEDPKGEDEEIPEEELSLEDvQAE 959

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41327691   1002 REALERALARLERRHSAlqrhstlgmEIEEQRQKLASLNsgsrEQSGLQASLEAEQEALEKDQERLE 1068
Cdd:TIGR02169  960 LQRVEEEIRALEPVNML---------AIQEYEEVLKRLD----ELKEKRAKLEEERKAILERIEEYE 1013
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 695-1076 3.65e-08

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: 58.14  E-value: 3.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    695 KRQEEETFLR---VQEELQRL----KELNNN--------EKAEKFQ-IFQELDQLQ--------KEKDEQYAKLELEKKR 750
Cdd:TIGR02168  171 KERRKETERKlerTRENLDRLedilNELERQlkslerqaEKAERYKeLKAELRELElallvlrlEELREELEELQEELKE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    751 LEEQEKEqvmlvahLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEaraggdedgeELEKaQLRFFEFKR 830
Cdd:TIGR02168  251 AEEELEE-------LTAELQELEEKLEELRL-EVSELEEEIEELQKELYALANEIS----------RLEQ-QKQILRERL 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    831 RQLVK-LVNLEKDLV---QQKDILKKEVQEEQEILECLKCEHDkesRLLEKHDESVtdvtevpqdfEKIKPVEYRLQYKE 906
Cdd:TIGR02168  312 ANLERqLEELEAQLEeleSKLDELAEELAELEEKLEELKEELE---SLEAELEELE----------AELEELESRLEELE 378

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    907 RQLQYLlqnhlptlleeKQRAFEILdrgplsldntlyqvekemeekeeqlAQYQANANQLQKLQATFEftaNIARQEEKV 986
Cdd:TIGR02168  379 EQLETL-----------RSKVAQLE-------------------------LQIASLNNEIERLEARLE---RLEDRRERL 419

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    987 RKKEKEILESREKQQREALERALARLER-RHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQE 1065
Cdd:TIGR02168  420 QQEIEELLKKLEEAELKELQAELEELEEeLEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499

                          410
                   ....*....|.
gi 41327691   1066 RLEYEIQQLKQ 1076
Cdd:TIGR02168  500 NLEGFSEGVKA 510
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 612-896 3.70e-08

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: 58.16  E-value: 3.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    612 KRKLIEEM------EEKQKSDKAELErmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLAEKEKFEEERLR 685
Cdd:TIGR02169  155 RRKIIDEIagvaefDRKKEKALEELE----EVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYELL 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    686 EQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELE-KKRLEEQEKEQVMLVAH 764
Cdd:TIGR02169  230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERS 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    765 LEEQLREKQEMIQLLRRGEVQwVEEEKRDLEGIRESLLRVKEARaggDEDGEELEKaqlrffefKRRQLVKLVNLEKDLV 844
Cdd:TIGR02169  310 IAEKERELEDAEERLAKLEAE-IDKLLAEIEELEREIEEERKRR---DKLTEEYAE--------LKEELEDLRAELEEVD 377

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 41327691    845 QQKDILKKEVQEEQEILECLKCEHD----KESRLLEKHDESVTDVTEVPQDFEKIK 896
Cdd:TIGR02169  378 KEFAETRDELKDYREKLEKLKREINelkrELDRLQEELQRLSEELADLNAAIAGIE 433
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
 1214-1269 4.10e-08

The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Yeast MDM1p is a filament-like protein localized in punctate structures distributed throughout the cytoplasm. It plays an important role in nuclear and mitochondrial transmission to daughter buds. Members of this subfamily show similar domain architectures as some sorting nexins (SNXs). Some members are similar to SNX19 in that they contain an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. Others are similar to SNX13 and SNX14, which also harbor these three domains as well as a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132786  Cd Length: 133  Bit Score: 53.47  E-value: 4.10e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 41327691 1214 TWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDER--VIAERRSHLEKYLR 1269
Cdd:cd06876   56 GWVVARRYSEFLELHKYLKKRYPGVLKLDFPQKRKISLKYSKtlLVEERRKALEKYLQ 113
PX_SNX20_21_like cd07279
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ...
 1219-1269 4.10e-08

The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX20, SNX21, and similar proteins. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. It may function in the sorting and cycling of PSGL-1 into endosomes. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.


Pssm-ID: 132812  Cd Length: 112  Bit Score: 52.72  E-value: 4.10e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 41327691 1219 RRYSRFREMHKTLKLKY-AELAALEFPPKKLFGNKDERVIAERRSHLEKYLR 1269
Cdd:cd07279   40 RRYSDFLKLYKALRKQHpQLMAKVSFPRKVLMGNFSSELIAERSRAFEQFLG 91
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 544-878 4.14e-08

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: 58.14  E-value: 4.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    544 GRTNMFRFNHPKEAAKLREKRKSGLLSSFSLSM--TDLSKSRENLsavmlynpglefeRQQREELEK-LESKRKLIEEME 620
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKalAELRKELEEL-------------EEELEQLRKeLEELSRQISALR 732

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    621 EkqksDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEERLREQQEIELQKKRQEE- 699
Cdd:TIGR02168  733 K----DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEl 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    700 --------ETFLRVQEELQRLKelnnNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLRE 771
Cdd:TIGR02168  809 raeltllnEEAANLRERLESLE----RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    772 KQEMIQLLRRgevqwvEEEKRDlEGIRESLLRVKEARAGGDEDGEELEKAQLRffefkrrqlvkLVNLEKDLVQQKDILK 851
Cdd:TIGR02168  885 LEEALALLRS------ELEELS-EELRELESKRSELRRELEELREKLAQLELR-----------LEGLEVRIDNLQERLS 946

                          330       340
                   ....*....|....*....|....*..
gi 41327691    852 KEVQEEQEILECLKCEHDKESRLLEKH 878
Cdd:TIGR02168  947 EEYSLTLEEAEALENKIEDDEEEARRR 973
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
600-1072 5.20e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.47  E-value: 5.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  600 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSfhIENKLKDLLAEKEKF 679
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA--LEAELAELPERLEEL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  680 EEERLREQQEIELQKKRQEEETflRVQEELQRLKELNNNEKAEKFQIF----QELDQLQKEKDEQYAKLELEKKRLEEQE 755
Cdd:COG4717  152 EERLEELRELEEELEELEAELA--ELQEELEELLEQLSLATEEELQDLaeelEELQQRLAELEEELEEAQEELEELEEEL 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  756 K--EQVMLVAHLEEQLREKQEMIQLLRRGEVqwveeekrdLEGIRESLLRVKEARAGgdedgeeLEKAQLRFFefkrrQL 833
Cdd:COG4717  230 EqlENELEAAALEERLKEARLLLLIAAALLA---------LLGLGGSLLSLILTIAG-------VLFLVLGLL-----AL 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  834 VKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKhDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQyll 913
Cdd:COG4717  289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPP-DLSPEELLELLDRIEELQELLREAEELEEELQ--- 364

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  914 qnhlptLLEEKQRAFEILDRGPLSLDNTLYQvekemeeKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEI 993
Cdd:COG4717  365 ------LEELEQEIAALLAEAGVEDEEELRA-------ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE 431

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  994 LESRE--------KQQREALERALARLERRHSALQRhstlGMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQE 1065
Cdd:COG4717  432 EELEEleeeleelEEELEELREELAELEAELEQLEE----DGELAELLQELEELKAELRELAEEWAALKLALELLEEARE 507


                 ....*..
gi 41327691 1066 RLEYEIQ 1072
Cdd:COG4717  508 EYREERL 514
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 742-1078 6.54e-08

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: 57.37  E-value: 6.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    742 AKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEvqwvEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKA 821
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL----EELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    822 QLRFFEFK---RRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKikpv 898
Cdd:TIGR02168  756 LTELEAEIeelEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER---- 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    899 eyRLQYKERQLQYLLQNhlptlLEEKQRAFEILdrgplsldntlyqvekemeekEEQLAQYQAnanQLQKLQATFEFTAN 978
Cdd:TIGR02168  832 --RIAATERRLEDLEEQ-----IEELSEDIESL---------------------AAEIEELEE---LIEELESELEALLN 880

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    979 IARQEEKVRKKEKEILESREKQQREaLERALARLERRHSALQ-RHSTLGMEIEEQRQKLASLNSGSREQSGLQAS-LEAE 1056
Cdd:TIGR02168  881 ERASLEEALALLRSELEELSEELRE-LESKRSELRRELEELReKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeAEAL 959

                          330       340
                   ....*....|....*....|..
gi 41327691   1057 QEALEKDQERLEYEIQQLKQKI 1078
Cdd:TIGR02168  960 ENKIEDDEEEARRRLKRLENKI 981
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
691-1165 7.57e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.00  E-value: 7.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   691 ELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEqekeqvmlvahLEEQLR 770
Cdd:PRK03918  173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-----------LKEEIE 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   771 EKQEMIqLLRRGEVQWVEEEKRDLE-GIRESLLRVK--EARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQK 847
Cdd:PRK03918  242 ELEKEL-ESLEGSKRKLEEKIRELEeRIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   848 DILkKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQyllqnhlPTLLEEKQRA 927
Cdd:PRK03918  321 EEI-NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLT-------GLTPEKLEKE 392

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   928 FEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQA---------TFEFTANIARQEEKVRKKEKEILESRE 998
Cdd:PRK03918  393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIE 472

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   999 KQQREaLERALARLER---RHSALQRHSTLGMEIEEQRQKLASLNSGSREQS--------GLQASLEAEQEALEKDQER- 1066
Cdd:PRK03918  473 EKERK-LRKELRELEKvlkKESELIKLKELAEQLKELEEKLKKYNLEELEKKaeeyeklkEKLIKLKGEIKSLKKELEKl 551

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  1067 --LEYEIQQLKQKIYEVDGVQKDHHGTLEGKVASSSLPVSAEKSHLVPLMdariNAYIE--------EEVQRRLQDLHRV 1136
Cdd:PRK03918  552 eeLKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFY----NEYLElkdaekelEREEKELKKLEEE 627

                         490       500
                  ....*....|....*....|....*....
gi 41327691  1137 ISEGCSTSADTMKDNEKLHNGTIQRKLKY 1165
Cdd:PRK03918  628 LDKAFEELAETEKRLEELRKELEELEKKY 656
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
 1198-1268 7.84e-08

The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Cytokine-independent survival kinase (CISK), also called Serum- and Glucocorticoid-induced Kinase 3 (SGK3), plays a role in cell growth and survival. It is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. CISK/SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. N-terminal to a catalytic kinase domain, CISK contains a PX domain which binds highly phosphorylated PIs, directs membrane localization, and regulates the enzyme's activity.


Pssm-ID: 132780  Cd Length: 109  Bit Score: 51.64  E-value: 7.84e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41327691 1198 KDAHFE-FEVKITVLDETWTVFRRYSRFREMHKTLKLKYAELaALEFPPKKLFGNK-DERVIAERRSHLEKYL 1268
Cdd:cd06870   16 KKKRFTvYKVVVSVGRSSWFVFRRYAEFDKLYESLKKQFPAS-NLKIPGKRLFGNNfDPDFIKQRRAGLDEFI 87
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 608-822 1.02e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.61  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  608 KLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKrrsfhienKLKDLLAEKEKfeeerlreq 687
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID--------KLQAEIAEAEA--------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  688 qeiELQKKRQEEETFLRVQEE--------------------LQRLKELNNNEKAEKfQIFQELDQLQKEKDEQYAKLELE 747
Cdd:COG3883   80 ---EIEERREELGERARALYRsggsvsyldvllgsesfsdfLDRLSALSKIADADA-DLLEELKADKAELEAKKAELEAK 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41327691  748 KKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQ 822
Cdd:COG3883  156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSA-EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 597-1077 1.77e-07

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: 55.75  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    597 EFERQQREELEKLESKRKLIEEMEEKQKSDK-------------AELERMQQEVETQRKETEIVQLQirkqeeslkRRSF 663
Cdd:TIGR00618  233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKqlrarieelraqeAVLEETQERINRARKAAPLAAHI---------KAVT 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    664 HIENKLKDLLAE-KEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQlQKEKDEQYA 742
Cdd:TIGR00618  304 QIEQQAQRIHTElQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ-QHTLTQHIH 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    743 KLELEKKRLEEQEKeqvmLVAHLEEQLREkqemiqllrrgevqwvEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQ 822
Cdd:TIGR00618  383 TLQQQKTTLTQKLQ----SLCKELDILQR----------------EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL 442

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    823 LRFFEFKRRQLVKLVNLEKDLVQQKdilkkeVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEVPqdfekiKPVEYRL 902
Cdd:TIGR00618  443 CAAAITCTAQCEKLEKIHLQESAQS------LKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP------CPLCGSC 510

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    903 QYKERQLQYLLqnhlptLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQanaNQLQKLQATFEFTA----- 977
Cdd:TIGR00618  511 IHPNPARQDID------NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK---EQMQEIQQSFSILTqcdnr 581

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    978 -----NIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLnsgSREQSGLQAS 1052
Cdd:TIGR00618  582 skediPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAL---HALQLTLTQE 658

                          490       500
                   ....*....|....*....|....*
gi 41327691   1053 LEAEQEALEKDQERLEYEIQQLKQK 1077
Cdd:TIGR00618  659 RVREHALSIRVLPKELLASRQLALQ 683
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 599-859 1.83e-07

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: 54.92  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    599 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQI--RKQEESLKRRSFHIENKLKDLLAEK 676
Cdd:pfam13868   30 EKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIeeREQKRQEEYEEKLQEREQMDEIVER 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    677 EKFEEERLREQQEIELQKKRQEEETFLRVQE---ELQRLKELNNNEKAEKFqifqeldqlQKEKDEQYAKLELEKKRL-E 752
Cdd:pfam13868  110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAewkELEKEEEREEDERILEY---------LKEKAEREEEREAEREEIeE 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    753 EQEKEQVMLVAHLEEQLREKQEMIQLLRRG-----EVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLR--- 824
Cdd:pfam13868  181 EKEREIARLRAQQEKAQDEKAERDELRAKLyqeeqERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEree 260

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 41327691    825 -FFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQE 859
Cdd:pfam13868  261 eEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELE 296
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 695-1083 1.95e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  695 KRQEEETFLR---VQEELQRLK----ELNNN--------EKAEKFQifqELDQLQKEKDEQYAKLELEKKRLEEQEKEQV 759
Cdd:COG1196  171 KERKEEAERKleaTEENLERLEdilgELERQleplerqaEKAERYR---ELKEELKELEAELLLLKLRELEAELEELEAE 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  760 mlVAHLEEQLREKQEMIQLLRRgevqwveeekrdlegiresllRVKEARAGGDEDGEELEKAQLRFFEFKRRQLvklvnl 839
Cdd:COG1196  248 --LEELEAELEELEAELAELEA---------------------ELEELRLELEELELELEEAQAEEYELLAELA------ 298

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  840 ekDLVQQKDILKKEVQEEQEILEclkcEHDKESRLLEKHDEsvtdvtevpqdfekikpveyrlqykerqlqyLLQNHLPT 919
Cdd:COG1196  299 --RLEQDIARLEERRRELEERLE----ELEEELAELEEELE-------------------------------ELEEELEE 341

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  920 LLEEKQRAFEILDrgplsldntlyqvekemeEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREK 999
Cdd:COG1196  342 LEEELEEAEEELE------------------EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691 1000 QQREALERALARLERRHSALQRHSTlgmEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIY 1079
Cdd:COG1196  404 ELEEAEEALLERLERLEEELEELEE---ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480


                 ....
gi 41327691 1080 EVDG 1083
Cdd:COG1196  481 ELLE 484
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
471-551 3.46e-07

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 49.57  E-value: 3.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  471 YHLKEGQTYVGRDDASteqDIVLHGLDLESEHCIFENIGGTVTLIPLsGSQ--CSVNGVQIVEATHLNQGAVILLGRTnM 548
Cdd:COG1716   16 FPLDGGPLTIGRAPDN---DIVLDDPTVSRRHARIRRDGGGWVLEDL-GSTngTFVNGQRVTEPAPLRDGDVIRLGKT-E 90


                 ...
gi 41327691  549 FRF 551
Cdd:COG1716   91 LRF 93
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 555-880 4.03e-07

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: 54.98  E-value: 4.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    555 KEAAKLREKRKSGLLSSFSLSMTDLSKSRENLSAVMLynpgLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQ 634
Cdd:pfam02463  691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRV----QEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEK 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    635 QEVETQRKETEIVQLQIRKQeeSLKRRSFHIENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEEtflrvQEELQRLKE 714
Cdd:pfam02463  767 SELSLKEKELAEEREKTEKL--KVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI-----KEEELEELA 839

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    715 LNNNEKAEKFQIFQELDQLQKEKDEQ--YAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQ------- 785
Cdd:pfam02463  840 LELKEEQKLEKLAEEELERLEEEITKeeLLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLeekenei 919

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    786 --WVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILEC 863
Cdd:pfam02463  920 eeRIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999

                          330
                   ....*....|....*..
gi 41327691    864 LKCEHDKESRLLEKHDE 880
Cdd:pfam02463 1000 LEEEKKKLIRAIIEETC 1016
PX_SNX22 cd06880
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ...
 1184-1268 4.38e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX22 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. The biological function of SNX22 is not yet known.


Pssm-ID: 132790  Cd Length: 110  Bit Score: 49.58  E-value: 4.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691 1184 IKISIP--RYVLCGQGKdAHFEFEVKITVLDETWTVFRRYSRFREMHKTLKLKYaelAALEFPPKKLfGNKDERVIAERR 1261
Cdd:cd06880    1 IEVSIPsyRLEVDESEK-PYTVFTIEVLVNGRRHTVEKRYSEFHALHKKLKKSI---KTPDFPPKRV-RNWNPKVLEQRR 75


                 ....*..
gi 41327691 1262 SHLEKYL 1268
Cdd:cd06880   76 QGLEAYL 82
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
595-1080 5.24e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 54.28  E-value: 5.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   595 GLEFERQQ-REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQE----------ESLKRRSF 663
Cdd:PRK02224  210 GLESELAElDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETErereelaeevRDLRERLE 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   664 HIENKLKDLLAEKEKFEEERLREQQEIELQKKRqEEETFLRVQEELQRLKELNNNEKAEKFQIfQELDQLQKEKDEQYAK 743
Cdd:PRK02224  290 ELEEERDDLLAEAGLDDADAEAVEARREELEDR-DEELRDRLEECRVAAQAHNEEAESLREDA-DDLEERAEELREEAAE 367

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   744 LELEKKRLEEQEKEQVMLVAHLEEQLREKqemiqllrRGEVQWVEEEKRDLEGIRESLLrvkEARAGGDEDGEELEkaql 823
Cdd:PRK02224  368 LESELEEAREAVEDRREEIEELEEEIEEL--------RERFGDAPVDLGNAEDFLEELR---EERDELREREAELE---- 432

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   824 rffefkrrqlVKLVNLEKDlvqqkdilkkeVQEEQEILE---CLKCEHD-KESRLLEKHDESVTDVTEVPQDFEKIKPVE 899
Cdd:PRK02224  433 ----------ATLRTARER-----------VEEAEALLEagkCPECGQPvEGSPHVETIEEDRERVEELEAELEDLEEEV 491

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   900 YRLQYKERQLQYL--LQNHLPTLLEEKQRAFEILDRGPLSLDNTlyqvekemeekEEQLAQYQANANQLQKLQATFEFTA 977
Cdd:PRK02224  492 EEVEERLERAEDLveAEDRIERLEERREDLEELIAERRETIEEK-----------RERAEELRERAAELEAEAEEKREAA 560

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   978 NIARQEEKVRKKEKEILESRE---KQQREALERALARLERRHSALQRHSTLgmeiEEQRQKLASLNSGSREQ-------- 1046
Cdd:PRK02224  561 AEAEEEAEEAREEVAELNSKLaelKERIESLERIRTLLAAIADAEDEIERL----REKREALAELNDERRERlaekrerk 636

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 41327691  1047 SGLQASLEAEQ-EALEKDQERLEYEIQQLKQKIYE 1080
Cdd:PRK02224  637 RELEAEFDEARiEEAREDKERAEEYLEQVEEKLDE 671
PX_SNX15_like cd06881
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX ...
 1216-1268 5.42e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily have similarity to sorting nexin 15 (SNX15), which contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein. Other members of this subfamily contain an additional C-terminal kinase domain, similar to human RPK118, which binds sphingosine kinase and the antioxidant peroxiredoxin-3 (PRDX3). RPK118 may be involved in the transport of proteins such as PRDX3 from the cytoplasm to its site of function in the mitochondria.


Pssm-ID: 132791  Cd Length: 117  Bit Score: 49.63  E-value: 5.42e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41327691 1216 TVFRRYSRFREMHKTLKLKYAELAALE----FPPKKLFGNKDERVIAERRSHLEKYL 1268
Cdd:cd06881   39 VVWKRYSDFKKLHRELSRLHKQLYLSGsfppFPKGKYFGRFDAAVIEERRQAILELL 95
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 601-1095 6.18e-07

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 53.96  E-value: 6.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    601 QQREELEKLESKRKL----IEEMEEKQKSDKAELE----RMQQEVETQRKETEIVQLQIR-----------KQEESLKRR 661
Cdd:pfam05483  265 ESRDKANQLEEKTKLqdenLKELIEKKDHLTKELEdikmSLQRSMSTQKALEEDLQIATKticqlteekeaQMEELNKAK 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    662 SFH--IENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEEtFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE 739
Cdd:pfam05483  345 AAHsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME-LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDE 423

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    740 QyAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGD----EDG 815
Cdd:pfam05483  424 K-KQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDklllENK 502

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    816 EELEKAQLRFFEFKRRQlVKLVNLEKdlvqQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTdvTEVPQDFEKI 895
Cdd:pfam05483  503 ELTQEASDMTLELKKHQ-EDIINCKK----QEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVK--CKLDKSEENA 575

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    896 KPVEYRLQYKERQLQYLLQ--NHLPTLLEEKQRAFEILDRGPLSLdntlyqvEKEMEEKEEQLAQYQANANQLQ-----K 968
Cdd:pfam05483  576 RSIEYEVLKKEKQMKILENkcNNLKKQIENKNKNIEELHQENKAL-------KKKGSAENKQLNAYEIKVNKLElelasA 648

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    969 LQATFEFTANIARQEEKVRKKEKEILESREKQ----------QREALERALARLERRHSALQRHS-TLGMEIEEQRQKLA 1037
Cdd:pfam05483  649 KQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAkaiadeavklQKEIDKRCQHKIAEMVALMEKHKhQYDKIIEERDSELG 728

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 41327691   1038 SLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQKDHHGTLEGK 1095
Cdd:pfam05483  729 LYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 597-808 6.57e-07

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: 53.92  E-value: 6.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    597 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQI---RKQEESLKRRSFH-----IENK 668
Cdd:TIGR02169  720 EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhklEEALNDLEARLSHsripeIQAE 799

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    669 LKDLlaEKEKFEEERLREQQEIELQKKRQEEETflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEK 748
Cdd:TIGR02169  800 LSKL--EEEVSRIEARLREIEQKLNRLTLEKEY---LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41327691    749 KRLEEQEKEQVML---VAHLEEQLREKQEmiqllRRGEVQWVEEEKRDLEGIRESLLRVKEAR 808
Cdd:TIGR02169  875 AALRDLESRLGDLkkeRDELEAQLRELER-----KIEELEAQIEKKRKRLSELKAKLEALEEE 932
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
 451-554 6.81e-07

forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing protein (Radil)-like family; The Radil-like family includes Radil and Ras-interacting protein 1 (Rain). Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility by linking Rap1 to beta2-integrin activation. Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. Both Radil and Rain contain an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438764 [Multi-domain]  Cd Length: 120  Bit Score: 49.61  E-value: 6.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  451 SELPHLIGI-----DDDLLstgiiLYHLKEGQTYVGRDDASTEQ-DIVLHGLDLESEHCI-----------FENIGGT-- 511
Cdd:cd22712    1 SDYPYLLTLrgfspKQDLL-----VYPLLEQVILVGSRTEGARKvDISLRAPDILPQHCWirrkpeplsddEDSDKESad 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 41327691  512 --VTLIPLSGSQCSVNGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22712   76 yrVVLSPLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
PTZ00121 PTZ00121
MAEBL; Provisional
 598-880 7.25e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 7.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   598 FERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEV---ETQRKETEIVQLQIRKQEESLKRrsfhIENKLKdllA 674
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaEEARKAEDAKRVEIARKAEDARK----AEEARK---A 1172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   675 EKEKfeeerlreqqeiELQKKRQEEEtfLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKL--ELEKKRLE 752
Cdd:PTZ00121 1173 EDAK------------KAEAARKAEE--VRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvkKAEEAKKD 1238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   753 EQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQ 832
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD 1318

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 41327691   833 LVKlvNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDE 880
Cdd:PTZ00121 1319 EAK--KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 600-776 1.03e-06

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: 51.46  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  600 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDLLAEKEKF 679
Cdd:COG1579    3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  680 EEERLREQQE---------IELQKKRQE--EETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEK 748
Cdd:COG1579   79 EEQLGNVRNNkeyealqkeIESLKRRISdlEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158

                        170       180
                 ....*....|....*....|....*...
gi 41327691  749 KRLEEQEKEqvmLVAHLEEQLREKQEMI 776
Cdd:COG1579  159 EELEAEREE---LAAKIPPELLALYERI 183
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
628-1132 1.50e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  628 AELERMQQEVETQRKETEIVQlQIRKQEESLKRrsfhienkLKDLLAEKEKFEEERLREQQEIELQKKRQEEEtflRVQE 707
Cdd:COG4913  235 DDLERAHEALEDAREQIELLE-PIRELAERYAA--------ARERLAELEYLRAALRLWFAQRRLELLEAELE---ELRA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  708 ELQRLKELNNNEKAEKFQIFQELDQLQKEKDE----QYAKLELEKKRLEEQEKEQVMLVAHLEEQLR-------EKQEMI 776
Cdd:COG4913  303 ELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAalglplpASAEEF 382

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  777 QLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEkAQLRffEFKRRQlvklVNLEKDLVQQKDILKK---- 852
Cdd:COG4913  383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE-AEIA--SLERRK----SNIPARLLALRDALAEalgl 455

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  853 ------------EVQEEQEI----LEclKCEHDKESRLL--EKHDESVTD---------------VTEVPQDFEKIKPVE 899
Cdd:COG4913  456 deaelpfvgeliEVRPEEERwrgaIE--RVLGGFALTLLvpPEHYAAALRwvnrlhlrgrlvyerVRTGLPDPERPRLDP 533

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  900 ----YRLQYKERQLQYLLQNHL-----------PTLLEEKQRA-------------FEILDRGPLS------LDNTlyqv 945
Cdd:COG4913  534 dslaGKLDFKPHPFRAWLEAELgrrfdyvcvdsPEELRRHPRAitragqvkgngtrHEKDDRRRIRsryvlgFDNR---- 609

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  946 ekemeekeEQLAQYQAnanQLQKLQATFEFTANIARQEekvrkkekeileSREKQQREALERALARLERRHSALQRHSTL 1025
Cdd:COG4913  610 --------AKLAALEA---ELAELEEELAEAEERLEAL------------EAELDALQERREALQRLAEYSWDEIDVASA 666

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691 1026 GMEIEEQRQKLASLNSGSREQSGLQASLE---AEQEALEKDQERLEYEIQQLKQKIYEVDGVQKDHHGTLEGKVAssslp 1102
Cdd:COG4913  667 EREIAELEAELERLDASSDDLAALEEQLEeleAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED----- 741

                        570       580       590
                 ....*....|....*....|....*....|
gi 41327691 1103 vsAEKSHLVPLMDARINAYIEEEVQRRLQD 1132
Cdd:COG4913  742 --LARLELRALLEERFAAALGDAVERELRE 769
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 580-795 3.41e-06

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: 51.49  E-value: 3.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    580 SKSRENLSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMqqEVETQRKETEivqLQIRKQEESLK 659
Cdd:pfam15709  295 GRSSPTQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRL--EVERKRREQE---EQRRLQQEQLE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    660 RrsfhiENKLkdllaeKEKFEEERLREQQEIELQKKRQEEETFLRVQEEL-QRLKELNNNEKAEKFQ--IFQELDQLQKE 736
Cdd:pfam15709  370 R-----AEKM------REELELEQQRRFEEIRLRKQRLEEERQRQEEEERkQRLQLQAAQERARQQQeeFRRKLQELQRK 438

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41327691    737 KDEQYA-KLELEKKRLEEQE----KEQVMLVAHLEEQ----LREKQEMIQllrrgEVQWVEEEKRDLE 795
Cdd:pfam15709  439 KQQEEAeRAEAEKQRQKELEmqlaEEQKRLMEMAEEErleyQRQKQEAEE-----KARLEAEERRQKE 501
PX_SNX19_like_plant cd06872
The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; ...
 1208-1270 3.57e-06

The phosphoinositide binding Phox Homology domain of uncharacterized SNX19-like plant proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized plant proteins containing an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some sorting nexins (SNXs). This is the same domain architecture found in SNX19. SNX13 and SNX14 also contain these three domains but also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.


Pssm-ID: 132782  Cd Length: 107  Bit Score: 47.13  E-value: 3.57e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41327691 1208 ITVLD---ETWTVFRRYSRFREMHKtlKLKYAELAALEFPPKKLFGNK-DERVIAERRSHLEKYLRD 1270
Cdd:cd06872   23 VAVTDnenETWVVKRRFRNFETLHR--RLKEVPKYNLELPPKRFLSSSlDGAFIEERCKLLDKYLKD 87
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
578-1084 5.26e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 5.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   578 DLSKSRENLSAVMlynpglefeRQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVetqrKETEIVQLQIRKQEES 657
Cdd:PRK03918  159 DYENAYKNLGEVI---------KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI----NEISSELPELREELEK 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   658 LKRRSFHIEnKLKDLLAEKEKFEEERLREQQEIELQKKRQEEetflRVQEELQRLKELNNNEKaekfqifqELDQLqKEK 737
Cdd:PRK03918  226 LEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEE----RIEELKKEIEELEEKVK--------ELKEL-KEK 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   738 DEQYAKLELE----KKRLEEQEKEqvmlVAHLEEQLREKQEMIQLL--RRGEVQWVEEE----KRDLEGIRESLLRVKEA 807
Cdd:PRK03918  292 AEEYIKLSEFyeeyLDELREIEKR----LSRLEEEINGIEERIKELeeKEERLEELKKKlkelEKRLEELEERHELYEEA 367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   808 RAGGDE--------DGEELEKAQLRFFEFKRRQLvKLVNLEKDLVQQKDILKKEVQEEQEILECLK-------------C 866
Cdd:PRK03918  368 KAKKEElerlkkrlTGLTPEKLEKELEELEKAKE-EIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgrelT 446

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   867 EHDKEsRLLEKHDESVTDVTEvpqDFEKIKPVEYRLQYKERQLQYLLQNHlPTLLEEKQRAFEIldrgpLSLDNTLYQVe 946
Cdd:PRK03918  447 EEHRK-ELLEEYTAELKRIEK---ELKEIEEKERKLRKELRELEKVLKKE-SELIKLKELAEQL-----KELEEKLKKY- 515

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   947 kemeekeeqlaqyqaNANQLQKLQATFEFTANIARQEEKVRKKEKEILESRE--KQQREALERALARLERRHSALQRH-S 1023
Cdd:PRK03918  516 ---------------NLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelKKKLAELEKKLDELEEELAELLKElE 580

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41327691  1024 TLGME-IEEQRQKLASLNSGSREQSGLQASlEAEQEALEKDQERLEYEIQQLKQKIYEVDGV 1084
Cdd:PRK03918  581 ELGFEsVEELEERLKELEPFYNEYLELKDA-EKELEREEKELKKLEEELDKAFEELAETEKR 641
PX_SNX25 cd06878
The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a ...
 1215-1268 5.34e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 25; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. The function of SNX25 is not yet known. It has been found in exosomes from human malignant pleural effusions. SNX25 shows the same domain architecture as SNX13 and SNX14, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.


Pssm-ID: 132788  Cd Length: 127  Bit Score: 46.98  E-value: 5.34e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 41327691 1215 WTVFRRYSRFREMHKTLKLKYAELAALEFP--PKKLFGNKDERVIAERRSHLEKYL 1268
Cdd:cd06878   50 WVVTRKLSEFHDLHRKLKECSSWLKKVELPslSKKWFKSIDKKFLDKSKNQLQKYL 105
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 599-792 5.55e-06

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: 50.15  E-value: 5.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  599 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRR-----SFHIENKLKDLL 673
Cdd:COG4942   47 KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyRLGRQPPLALLL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  674 AEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQE-------LDQLQKEKDEQYAKLEL 746
Cdd:COG4942  127 SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEleeeraaLEALKAERQKLLARLEK 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 41327691  747 EKKRLEEQekeqvmlvahLEEQLREKQEMIQLLRRGEVQWVEEEKR 792
Cdd:COG4942  207 ELAELAAE----------LAELQQEAEELEALIARLEAEAAAAAER 242
PX_SNX20 cd07300
The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a ...
 1219-1274 5.85e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. The PX domain of SNX20 binds PIs and targets the SNX20/PSGL-1 complex to endosomes. SNX20 may function in the sorting and cycling of PSGL-1 into endosomes.


Pssm-ID: 132833  Cd Length: 114  Bit Score: 46.73  E-value: 5.85e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41327691 1219 RRYSRFREMHKTLKLKYAE-LAALEFPPKKLFGNKDERVIAERRSHLEKYLRDFFSV 1274
Cdd:cd07300   40 RRYSDFLKLHQELLSDFSEeLEDVVFPKKKLTGNFSEEIIAERRVALRDYLTLLYSL 96
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
616-771 8.95e-06

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 50.24  E-value: 8.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  616 IEEMEEKQKSDkaELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIEnKLKDLLAEKEKfeeerLREQQEIELQKK 695
Cdd:COG2433  382 LEELIEKELPE--EEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE-ELEAELEEKDE-----RIERLERELSEA 453

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41327691  696 RQEEETFLRVQEELQRLKELNNNEKAEkfqifqeLDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLRE 771
Cdd:COG2433  454 RSEERREIRKDREISRLDREIERLERE-------LEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKE 522
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
 471-555 1.28e-05

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 44.94  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    471 YHLKEGQTYVGRDDastEQDIVLHGLDLESEHCIFENIGGTVTLIPL-SGSQCSVNGVQIVEATH-LNQGAVILLGRTnM 548
Cdd:pfam16697   12 FPLEGGRYRIGSDP---DCDIVLSDKEVSRVHLKLEVDDEGWRLDDLgSGNGTLVNGQRVTELGIaLRPGDRIELGQT-E 87


                   ....*..
gi 41327691    549 FRFNHPK 555
Cdd:pfam16697   88 FCLVPAD 94
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 788-1089 1.28e-05

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: 50.06  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    788 EEEKRDLEGIRESLLRVKEARaggdedgEELEKaQLRFFEFKRRQLVKLVNLEKDLVQ-QKDILKKEVQEEQEILECLKc 866
Cdd:TIGR02168  175 KETERKLERTRENLDRLEDIL-------NELER-QLKSLERQAEKAERYKELKAELRElELALLVLRLEELREELEELQ- 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    867 ehDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNH------LPTLLEEKQRAFEILDRGPLSLDN 940
Cdd:TIGR02168  246 --EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALaneisrLEQQKQILRERLANLERQLEELEA 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    941 TLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEftaniarQEEKVRKKEKEILESREKQQREALERA------------ 1008
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEKLEELKEELESLE-------AELEELEAELEELESRLEELEEQLETLrskvaqlelqia 396

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   1009 -----LARLERRHSALQ-RHSTLGMEIEEQRQKL--ASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYE 1080
Cdd:TIGR02168  397 slnneIERLEARLERLEdRRERLQQEIEELLKKLeeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476


                   ....*....
gi 41327691   1081 VDGVQKDHH 1089
Cdd:TIGR02168  477 LDAAERELA 485
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
598-1078 1.34e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  598 FERQQREELEKLESKRKlieemeEKQKSDKAELERMQQEVETQRKETEIVQlQIRKQEESLKRRSFHIENKLKDLLAEKE 677
Cdd:COG4717   47 LLERLEKEADELFKPQG------RKPELNLKELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  678 KFEEERLREQQEIELQKKRQEEETF-LRVQEELQRLKELNNNEKAEKfQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 756
Cdd:COG4717  120 KLEKLLQLLPLYQELEALEAELAELpERLEELEERLEELRELEEELE-ELEAELAELQEELEELLEQLSLATEEELQDLA 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  757 EQVmlvAHLEEQLREKQEmiqllrrgEVQWVEEEKRDLEGIRESLlrvkEARAGGDEDGEELEKAQLRFFEFkrRQLVKL 836
Cdd:COG4717  199 EEL---EELQQRLAELEE--------ELEEAQEELEELEEELEQL----ENELEAAALEERLKEARLLLLIA--AALLAL 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  837 VNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEkhdesvtdvtevpQDFEKIKPVEYRLQYKERQLQYLLQNH 916
Cdd:COG4717  262 LGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG-------------KEAEELQALPALEELEEEELEELLAAL 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  917 LPTLLEEKQRAFEILDRgplsldntlyqvekemeekeeqLAQYQANANQLQKLQAtfeftaniARQEEKVRKKEKEILES 996
Cdd:COG4717  329 GLPPDLSPEELLELLDR----------------------IEELQELLREAEELEE--------ELQLEELEQEIAALLAE 378

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  997 REKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQ--ASLEAEQEALEKDQERLEYEIQQL 1074
Cdd:COG4717  379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEelEELEEELEELEEELEELREELAEL 458


                 ....
gi 41327691 1075 KQKI 1078
Cdd:COG4717  459 EAEL 462
PTZ00121 PTZ00121
MAEBL; Provisional
 599-1168 1.52e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   599 ERQQREELEKLESKRKLIE--EMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLKDllAEK 676
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKK----AEEAKKD--AEE 1241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   677 EKfeeerlreqqeiELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEK 756
Cdd:PTZ00121 1242 AK------------KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK 1309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   757 --EQVMLVAHLEEQLREKQEMIQLLRRG--EVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQ 832
Cdd:PTZ00121 1310 kaEEAKKADEAKKKAEEAKKKADAAKKKaeEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   833 LVKLVNLEKDLVQQK---DILKKEVQEEQEILEC-LKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQ 908
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKkkaDELKKAAAAKKKADEAkKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   909 LQyllQNHLPTLLEEKQRAFEI---LDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEK 985
Cdd:PTZ00121 1470 KK---ADEAKKKAEEAKKADEAkkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK 1546

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   986 VRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLASLNSGSREQSGLQASLEAEQ----EALE 1061
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikaEELK 1626

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  1062 KDQERLEYEIQQLKQKIYEVDGVQKDHHGTLEGKVASSSLPVSAE--KSHLVPLMDARINAYIEEEVQRRLQDLHRVISE 1139
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706

                         570       580
                  ....*....|....*....|....*....
gi 41327691  1140 GCSTSADTMKDNEKLHNGTIQRKLKYERM 1168
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 601-1074 2.27e-05

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: 49.20  E-value: 2.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    601 QQREELEKLESKRKLIEEMEEK--QKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 678
Cdd:TIGR00618  264 QLRARIEELRAQEAVLEETQERinRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    679 FEEERLREQQEIELQKKRQEEETFL----RVQEELQRLKELNNNEKA--EKFQIF-QELDQLQKEKDEQYAKL------- 744
Cdd:TIGR00618  344 RRLLQTLHSQEIHIRDAHEVATSIReiscQQHTLTQHIHTLQQQKTTltQKLQSLcKELDILQREQATIDTRTsafrdlq 423

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    745 ----------ELEKKRLEEQE-------KEQVMLVAHLEEQLREKQEMIQLLRRGEVQWV-EEEKRDLEGIRESLLRVKE 806
Cdd:TIGR00618  424 gqlahakkqqELQQRYAELCAaaitctaQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLqETRKKAVVLARLLELQEEP 503

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    807 ARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCE----HDKESRLLEKHDESV 882
Cdd:TIGR00618  504 CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQmqeiQQSFSILTQCDNRSK 583

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    883 TDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNHLPTLLEEkqrafeildrgplsLDNTLYQVEKEMEEKEEQLAQYQAN 962
Cdd:TIGR00618  584 EDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE--------------QDLQDVRLHLQQCSQELALKLTALH 649

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    963 ANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHSTLGMEIEEQRQKLAslNSG 1042
Cdd:TIGR00618  650 ALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE--NAS 727

                          490       500       510
                   ....*....|....*....|....*....|..
gi 41327691   1043 SREQSGLQASLEAEQEALEKDQERLEYEIQQL 1074
Cdd:TIGR00618  728 SSLGSDLAAREDALNQSLKELMHQARTVLKAR 759
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 640-832 2.80e-05

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: 46.84  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  640 QRKETEIVQlqIRKQEESLKRRsfhiENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEETFlRVQEELQRLKELNNNE 719
Cdd:COG1579   13 QELDSELDR--LEHRLKELPAE----LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-EVEARIKKYEEQLGNV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  720 KAEKfqifqELDQLQKEKDeqyaKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRE 799
Cdd:COG1579   86 RNNK-----EYEALQKEIE----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 41327691  800 SLLRVKEARAggdEDGEELEKAQLRFFEFKRRQ 832
Cdd:COG1579  157 ELEELEAERE---ELAAKIPPELLALYERIRKR 186
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 597-1015 5.82e-05

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 47.41  E-value: 5.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    597 EFERQQREELEKLESKRKLI-EEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENK------L 669
Cdd:pfam05483  331 EEKEAQMEELNKAKAAHSFVvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKeveleeL 410

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    670 KDLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQ------RLKELNNNEKAEKFQIFQELDQLQKEK------ 737
Cdd:pfam05483  411 KKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEihdleiQLTAIKTSEEHYLKEVEDLKTELEKEKlkniel 490

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    738 DEQYAKLELEKKRLEEQEKEQVM-LVAHLEEQLREKQEMIQLLRRGE-VQWVEEEKRD-LEGIRESLLRVKEARAGGDED 814
Cdd:pfam05483  491 TAHCDKLLLENKELTQEASDMTLeLKKHQEDIINCKKQEERMLKQIEnLEEKEMNLRDeLESVREEFIQKGDEVKCKLDK 570

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    815 GEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVT----DVTEVPQ 890
Cdd:pfam05483  571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNklelELASAKQ 650

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    891 DFEKIKPvEYRLQYKERQLQYllqnhlPTLLEEKQRAFEILDRGP------------------LSLDNTLYQVEKEMEEK 952
Cdd:pfam05483  651 KFEEIID-NYQKEIEDKKISE------EKLLEEVEKAKAIADEAVklqkeidkrcqhkiaemvALMEKHKHQYDKIIEER 723

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41327691    953 EEQLAQYQANANQLQKLQATFEFT-ANIARQEEKVRKKEKEILESREKQQREALERALARLERR 1015
Cdd:pfam05483  724 DSELGLYKNKEQEQSSAKAALEIElSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 601-1094 6.04e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 47.48  E-value: 6.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    601 QQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVEtqrKETEIVQLQIRKQEEslkrrsfhienklkdLLAEKEKFe 680
Cdd:pfam01576    2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLC---EEKNALQEQLQAETE---------------LCAEAEEM- 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    681 eerlreqqEIELQKKRQEEETFL-----RVQEELQRLKELnNNEKAEKFQIFQELDQ-----------LQKEK------- 737
Cdd:pfam01576   63 --------RARLAARKQELEEILhelesRLEEEEERSQQL-QNEKKKMQQHIQDLEEqldeeeaarqkLQLEKvtteaki 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    738 ----------DEQYAKLELEKKRLEEQEKEQVMLVAHLEE------QLREKQEMI-----QLLRRGEVQWVEEEK--RDL 794
Cdd:pfam01576  134 kkleedilllEDQNSKLSKERKLLEERISEFTSNLAEEEEkakslsKLKNKHEAMisdleERLKKEEKGRQELEKakRKL 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    795 EG--------IRESLLRVKEARAGGDEDGEELEKAQLRFFE--FKRRQLVK--------LVNLEKDLVQQKDILKKEVQE 856
Cdd:pfam01576  214 EGestdlqeqIAELQAQIAELRAQLAKKEEELQAALARLEEetAQKNNALKkireleaqISELQEDLESERAARNKAEKQ 293

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    857 EQ---EILECLKCE----HDKESRLLEKHDESVTDVTEVPqdfekiKPVEYRLQYKERQLQYLLQNHlPTLLEEKQRAFE 929
Cdd:pfam01576  294 RRdlgEELEALKTEledtLDTTAAQQELRSKREQEVTELK------KALEEETRSHEAQLQEMRQKH-TQALEELTEQLE 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    930 ILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANAN-----------QLQKLQATFEFTANIARQEEKVRKKEKEILESRE 998
Cdd:pfam01576  367 QAKRNKANLEKAKQALESENAELQAELRTLQQAKQdsehkrkklegQLQELQARLSESERQRAELAEKLSKLQSELESVS 446

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    999 KQQREAlERALARLERRHSAL--QRHSTLGMEIEEQRQKLA---SLNSGSREQSGLQASLEAEQEAlekdQERLEYEIQQ 1073
Cdd:pfam01576  447 SLLNEA-EGKNIKLSKDVSSLesQLQDTQELLQEETRQKLNlstRLRQLEDERNSLQEQLEEEEEA----KRNVERQLST 521

                          570       580
                   ....*....|....*....|.
gi 41327691   1074 LKQKIYEVDGVQKDHHGTLEG 1094
Cdd:pfam01576  522 LQAQLSDMKKKLEEDAGTLEA 542
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
607-1021 6.11e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 6.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  607 EKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIR----KQEESLKRRSFHIENKLKDLLAEKEKFEEE 682
Cdd:COG4913  288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEAL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  683 RLREQQEIELqkkrqEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQ----EKEQ 758
Cdd:COG4913  368 LAALGLPLPA-----SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRksniPARL 442

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  759 VMLVAHLEEQLREKQ-------EMIQLlRRGEVQW----------------VEEE----------KRDL------EGIRE 799
Cdd:COG4913  443 LALRDALAEALGLDEaelpfvgELIEV-RPEEERWrgaiervlggfaltllVPPEhyaaalrwvnRLHLrgrlvyERVRT 521

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  800 SLLRVKEARAGGD------------------------------EDGEELE------------KAQLRFFE-----FKRRQ 832
Cdd:COG4913  522 GLPDPERPRLDPDslagkldfkphpfrawleaelgrrfdyvcvDSPEELRrhpraitragqvKGNGTRHEkddrrRIRSR 601

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  833 LV-------KLVNLEKDLVQqkdiLKKEVQEEQEILEclkcEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYK 905
Cdd:COG4913  602 YVlgfdnraKLAALEAELAE----LEEELAEAEERLE----ALEAELDALQERREALQRLAEYSWDEIDVASAEREIAEL 673

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  906 ERQLQYLLQNH--LPTLLEEKQRAFEILDRgplsLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQE 983
Cdd:COG4913  674 EAELERLDASSddLAALEEQLEELEAELEE----LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749

                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 41327691  984 EKVRKKEKEILESREKQQREALERALARLERRHSALQR 1021
Cdd:COG4913  750 LLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
898-1085 6.44e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 6.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  898 VEYRLQYKERQLQY---LLQNHLPTL---LEEKQRAFEILDR--GPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKL 969
Cdd:COG3206  162 LEQNLELRREEARKaleFLEEQLPELrkeLEEAEAALEEFRQknGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  970 QATFEftANIARQEEKVRKKEKEILESREKQQREALERALARLERRHSAlqRHStlgmEIEEQRQKLASLNSG-SREQSG 1048
Cdd:COG3206  242 LAALR--AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTP--NHP----DVIALRAQIAALRAQlQQEAQR 313

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 41327691 1049 LQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQ 1085
Cdd:COG3206  314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 603-1013 6.90e-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: 47.66  E-value: 6.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    603 REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRsfhiENKLKDLLAEKEKFEEE 682
Cdd:pfam02463  615 ADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTK----ELLEIQELQEKAESELA 690

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    683 RLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEqyAKLELEKKRLEEQEKEQVMLV 762
Cdd:pfam02463  691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDE--EEEEEEKSRLKKEEKEEEKSE 768

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    763 AHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFfEFKRRQLVKLVNLEKD 842
Cdd:pfam02463  769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIK-EEELEELALELKEEQK 847

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    843 LVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVT-DVTEVPQDFEKIKPVEYRLQYK--ERQLQYLLQNHLPT 919
Cdd:pfam02463  848 LEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELeSKEEKEKEEKKELEEESQKLNLleEKENEIEERIKEEA 927

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    920 LLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREK 999
Cdd:pfam02463  928 EILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007

                          410
                   ....*....|....
gi 41327691   1000 QQREALERALARLE 1013
Cdd:pfam02463 1008 IRAIIEETCQRLKE 1021
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
 1201-1270 7.21e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles.


Pssm-ID: 132776  Cd Length: 105  Bit Score: 43.37  E-value: 7.21e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691 1201 HFEFEVKiTVLDETwTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERRSHLEKYLRD 1270
Cdd:cd06866   18 HVEYEVS-SKRFKS-TVYRRYSDFVWLHEYLLKRYPYRMVPALPPKRIGGSADREFLEARRRGLSRFLNL 85
PRK12704 PRK12704
phosphodiesterase; Provisional
 602-757 7.58e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.08  E-value: 7.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   602 QREELEKLESKRKLIEEMEEKQKSDKAELERmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEE 681
Cdd:PRK12704   45 EEAKKEAEAIKKEALLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41327691   682 ERLreqqeiELQKKRQEEETflRVQEELQRLKELNNNEKAEKFQIFqeLDQLQKEKDEQYAKL--ELEKKRLEEQEKE 757
Cdd:PRK12704  122 KQQ------ELEKKEEELEE--LIEEQLQELERISGLTAEEAKEIL--LEKVEEEARHEAAVLikEIEEEAKEEADKK 189
PX_PI3K_C2 cd06883
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The ...
 1212-1283 9.30e-05

The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are also involved in the regulation of clathrin-mediated membrane trafficking as well as ATP-dependent priming of neurosecretory granule exocytosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. Class II PI3Ks include three vertebrate isoforms (alpha, beta, and gamma), the Drosophila PI3K_68D, and similar proteins.


Pssm-ID: 132793  Cd Length: 109  Bit Score: 43.11  E-value: 9.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41327691 1212 DETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAERR-SHLEKYLRDFFSVMLQSATSPL 1283
Cdd:cd06883   29 TEPSFVFRTFEEFQELHNKLSLLFPSLKLPSFPARVVLGRSHIKQVAERRkIELNSYLKSLFNASPEVAESDL 101
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 590-1067 1.00e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 46.74  E-value: 1.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    590 MLYNPGLEFERQQREELEKLESKRKLIEEMEEKqksdkaeLERMQQEVetQRKETEIVQLQIR-----KQEESLKRrsfH 664
Cdd:pfam10174  258 MLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNK-------IDQLKQEL--SKKESELLALQTKletltNQNSDCKQ---H 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    665 IEnKLKDLLAEKEKfeEERLREQQEIELQKKRQEEETFL-RVQEELQRLKElnnnekaEKFQIFQELDQLQKEKDEQYAK 743
Cdd:pfam10174  326 IE-VLKESLTAKEQ--RAAILQTEVDALRLRLEEKESFLnKKTKQLQDLTE-------EKSTLAGEIRDLKDMLDVKERK 395

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    744 LELEKKRLEeqekeqvmlvaHLEEQLREKQEMIQLLRRGevqwVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQL 823
Cdd:pfam10174  396 INVLQKKIE-----------NLQEQLRDKDKQLAGLKER----VKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQRE 460

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    824 RFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQE-EQEILECLKCEHDKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRL 902
Cdd:pfam10174  461 REDRERLEELESLKKENKDLKEKVSALQPELTEkESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQL 540

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    903 QyKERQLQY-------------LLQNHLPTLLEEKQRAFEILDRgplsLDNTLYQVEKEMEEKEEQLAQYQANANQLQKL 969
Cdd:pfam10174  541 K-KAHNAEEavrtnpeindrirLLEQEVARYKEESGKAQAEVER----LLGILREVENEKNDKDKKIAELESLTLRQMKE 615

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    970 QATfeFTANI-ARQEEKVRKKEKEILESREKQQREALERALARLERRHSALQRHStlgMEIEEQRQKLASLNSGSREQSG 1048
Cdd:pfam10174  616 QNK--KVANIkHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTR---QELDATKARLSSTQQSLAEKDG 690

                          490       500
                   ....*....|....*....|....
gi 41327691   1049 LQASLEAE-----QEALEKDQERL 1067
Cdd:pfam10174  691 HLTNLRAErrkqlEEILEMKQEAL 714
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 604-820 1.19e-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: 46.60  E-value: 1.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    604 EELEKLESKRKLIEEMEEKQKsdkAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEER 683
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEI---QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    684 LREQQEIELQKKRQEEetflrVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEqyaklelekkrlEEQEKEQVMLVA 763
Cdd:TIGR02169  892 DELEAQLRELERKIEE-----LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE------------DEEIPEEELSLE 954

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41327691    764 HLEEQLREKQEMIQLLrrGEV-----QWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEK 820
Cdd:TIGR02169  955 DVQAELQRVEEEIRAL--EPVnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 599-859 1.44e-04

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


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 45.80  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    599 ERQQREELEKLESKRKLIEEMEEKQKsdkaeleRMQQEVETQRKEteivQLQIRKQEESLKRRsfHIENKLKDLLAEKEK 678
Cdd:pfam15558   72 ARLGREERRRADRREKQVIEKESRWR-------EQAEDQENQRQE----KLERARQEAEQRKQ--CQEQRLKEKEEELQA 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    679 FEEERLREQQEIELQ--KKRQEEETflrvqEELQRLKELNNNEKAEKFQIFQELDqLQKEKDEQYAKLELEKKRLEEQEK 756
Cdd:pfam15558  139 LREQNSLQLQERLEEacHKRQLKER-----EEQKKVQENNLSELLNHQARKVLVD-CQAKAEELLRRLSLEQSLQRSQEN 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    757 -EQVMLVAHLEEQLREKQEMIQLLRrgeVQWVEEEK-RDLEGIRESLLRVKEARAGGDEDGEELEKAQlrffefkRRQLV 834
Cdd:pfam15558  213 yEQLVEERHRELREKAQKEEEQFQR---AKWRAEEKeEERQEHKEALAELADRKIQQARQVAHKTVQD-------KAQRA 282

                          250       260
                   ....*....|....*....|....*
gi 41327691    835 KLVNLEKDLVQQkdILKKEVQEEQE 859
Cdd:pfam15558  283 RELNLEREKNHH--ILKLKVEKEEK 305
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 596-862 1.44e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.68  E-value: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    596 LEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRsfhIENKLKDLLAE 675
Cdd:pfam13868   91 EEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDER---ILEYLKEKAER 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    676 KEKFEeerlreqqeielQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELdqLQKEKDEQYAKLELEKKrlEEQE 755
Cdd:pfam13868  168 EEERE------------AEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKL--YQEEQERKERQKEREEA--EKKA 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    756 KEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAggdEDGEELEKAQLRFFEFKRRQLVK 835
Cdd:pfam13868  232 RQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRR---MKRLEHRRELEKQIEEREEQRAA 308

                          250       260
                   ....*....|....*....|....*..
gi 41327691    836 LVNLEkdlVQQKDILKKEVQEEQEILE 862
Cdd:pfam13868  309 EREEE---LEEGERLREEEAERRERIE 332
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 595-753 1.44e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  595 GLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLA 674
Cdd:COG1196  660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  675 EKEKFEEERLREQQEIELQKKRQEEetflrVQEELQRLK-ELNN----NEKAEkfqifQELDQLQKEKD---EQYAKLEL 746
Cdd:COG1196  740 ELLEEEELLEEEALEELPEPPDLEE-----LERELERLErEIEAlgpvNLLAI-----EEYEELEERYDflsEQREDLEE 809


                 ....*..
gi 41327691  747 EKKRLEE 753
Cdd:COG1196  810 ARETLEE 816
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 576-913 1.71e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 46.26  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    576 MTDLSKSRENLSAVMLYNPGLEFERQQ-REELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQrkETEIVQLQIR-- 652
Cdd:pfam15921  450 MAAIQGKNESLEKVSSLTAQLESTKEMlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT--NAEITKLRSRvd 527

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    653 ---KQEESLKRRSFHIEN------KLKDLLAEKEKFeeerlreqqeIELQKKRQEEETFLRVQ----------EELQRLK 713
Cdd:pfam15921  528 lklQELQHLKNEGDHLRNvqteceALKLQMAEKDKV----------IEILRQQIENMTQLVGQhgrtagamqvEKAQLEK 597

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    714 ELNNNEkaekfqifQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLRE----KQEMIQLLR-----RGEV 784
Cdd:pfam15921  598 EINDRR--------LELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAvkdiKQERDQLLNevktsRNEL 669

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    785 QWVEEE----KRDLEGIRESL--------LRVKEARAggdedgeELEKAQ--LRFFEFKRRQLVKL-VNLEKDLVQQK-- 847
Cdd:pfam15921  670 NSLSEDyevlKRNFRNKSEEMetttnklkMQLKSAQS-------ELEQTRntLKSMEGSDGHAMKVaMGMQKQITAKRgq 742

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41327691    848 -DILKKEVQ-EEQEILECLKCEH---DKESRLLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLL 913
Cdd:pfam15921  743 iDALQSKIQfLEEAMTNANKEKHflkEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 841-1078 2.30e-04

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: 45.14  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  841 KDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTEvpqdfeKIKPVEYRLQYKERQLQyllqnhlpTL 920
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR------RIRALEQELAALEAELA--------EL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  921 LEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREK- 999
Cdd:COG4942   89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAe 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691 1000 --QQREALERALARLERRHSALQRhstlgmEIEEQRQKLASLNSGsreqsglQASLEAEQEALEKDQERLEYEIQQLKQK 1077
Cdd:COG4942  169 leAERAELEALLAELEEERAALEA------LKAERQKLLARLEKE-------LAELAAELAELQQEAEELEALIARLEAE 235


                 .
gi 41327691 1078 I 1078
Cdd:COG4942  236 A 236
PX_SNX27 cd06886
The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a ...
 1219-1274 2.49e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexin 27; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX27 contains an N-terminal PDZ domain followed by a PX domain and a Ras-Associated (RA) domain. It binds G protein-gated potassium (Kir3) channels, which play a role in neuronal excitability control, through its PDZ domain. SNX27 downregulates Kir3 channels by promoting their movement in the endosome, reducing surface expression and increasing degradation. SNX27 also associates with 5-hydroxytryptamine type 4 receptor (5-HT4R), cytohesin associated scaffolding protein (CASP), and diacylglycerol kinase zeta, and may play a role in their intracellular trafficking and endocytic recycling. The SNX27 PX domain preferentially binds to phosphatidylinositol-3-phosphate (PI3P) and is important for targeting to the early endosome.


Pssm-ID: 132796  Cd Length: 106  Bit Score: 41.63  E-value: 2.49e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 41327691 1219 RRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERVIAeRRSHLEKYLRDFFSV 1274
Cdd:cd06886   36 RRYREFANLHQNLKKEFPDFQFPKLPGKWPFSLSEQQLDA-RRRGLEQYLEKVCSI 90
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
 1220-1268 2.59e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Members of this subfamily include sorting nexin 17 (SNX17), SNX31, and similar proteins. They contain an N-terminal PX domain followed by a truncated FERM (4.1, ezrin, radixin, and moesin) domain and a unique C-terminal region. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX17 is known to regulate the trafficking and processing of a number of proteins. It binds some members of the low-density lipoprotein receptor (LDLR) family such as LDLR, VLDLR, ApoER2, and others, regulating their endocytosis. It also binds P-selectin and may regulate its lysosomal degradation. SNX17 is highly expressed in neurons. It binds amyloid precursor protein (APP) and may be involved in its intracellular trafficking and processing to amyloid beta peptide, which plays a central role in the pathogenesis of Alzheimer's disease. The biological function of SNX31 is unknown.


Pssm-ID: 132795  Cd Length: 104  Bit Score: 41.55  E-value: 2.59e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 41327691 1220 RYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDERvIAERRSHLEKYL 1268
Cdd:cd06885   34 RYSQLHGLNEQLKKEFGNRKLPPFPPKKLLPLTPAQ-LEERRLQLEKYL 81
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
 473-551 2.71e-04

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 41.43  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  473 LKEGQTYVGRDDASteqDIVLHGLDLESEHC-IFENIGGTVTLIPLSGS-QCSVNGVQIVEATHLNQGAVILLGrTNMFR 550
Cdd:cd22673   18 LTKKSCTFGRDLSC---DIRIQLPGVSREHCrIEVDENGKAYLENLSTTnPTLVNGKAIEKSAELKDGDVITIG-GRSFR 93


                 .
gi 41327691  551 F 551
Cdd:cd22673   94 F 94
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
556-792 3.12e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.52  E-value: 3.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  556 EAAKLREKRKSGLLSsfslsMTDLSKSRENLSAVMlyNPGLEFERQQREELEKLESKRKLIEEMEEKQksdkAELERMQQ 635
Cdd:COG1340   58 EAQELREKRDELNEK-----VKELKEERDELNEKL--NELREELDELRKELAELNKAGGSIDKLRKEI----ERLEWRQQ 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  636 -EVETQRKETEIVQlQIRKQEESLKRR--SFHIENKLKDLLAEkekfeeerlreqqeieLQKKRQEEETFlrvQEELQRL 712
Cdd:COG1340  127 tEVLSPEEEKELVE-KIKELEKELEKAkkALEKNEKLKELRAE----------------LKELRKEAEEI---HKKIKEL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  713 KELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKR 792
Cdd:COG1340  187 AEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 478-543 3.19e-04

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 40.25  E-value: 3.19e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41327691    478 TYVGRDDastEQDIVLHGLDLESEHCIFENI-GGTVTLIPL-SGSQCSVNGVQIVEATH-LNQGAVILL 543
Cdd:pfam00498    1 VTIGRSP---DCDIVLDDPSVSRRHAEIRYDgGGRFYLEDLgSTNGTFVNGQRLGPEPVrLKDGDVIRL 66
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 550-752 3.51e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.11  E-value: 3.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    550 RFNHPKEAA---KLREKRKSGLLSSFSLSMTDLSKSRENLSAVMLY----NPGLEFERQQREELEKLESKRKLiEEMEEK 622
Cdd:pfam17380  393 RVRQELEAArkvKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRrleeERAREMERVRLEEQERQQQVERL-RQQEEE 471

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    623 QKSDKAELERMQQEvetQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEERLREQQEIELQKKR---QEE 699
Cdd:pfam17380  472 RKRKKLELEKEKRD---RKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERrkqQEM 548

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 41327691    700 ETFLRVQEELQRLKElnnnEKAekfqifqELDQLQKEKDEQYAKLELEKKRLE 752
Cdd:pfam17380  549 EERRRIQEQMRKATE----ERS-------RLEAMEREREMMRQIVESEKARAE 590
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 601-1138 4.05e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 44.83  E-value: 4.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    601 QQREELEKLESKRKLIEEMEEKQKsdkAELERMQQEVETQ-RKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEkf 679
Cdd:pfam12128  387 QNNRDIAGIKDKLAKIREARDRQL---AVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE-- 461

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    680 eeerlreqqeiELQKKRQEEETFLRVQEELQRlkelnNNEKAEKFQifQELDQLQKEKDEQYAKLELEKKRLEEQEKEqv 759
Cdd:pfam12128  462 -----------LLLQLENFDERIERAREEQEA-----ANAEVERLQ--SELRQARKRRDQASEALRQASRRLEERQSA-- 521

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    760 mlVAHLEEQLREKQ-EMIQLLRRGEVQWVEEEKRDLEgiRESLLR---VKEARAGGDEDGEELEKAQLRffeFKRRQLVK 835
Cdd:pfam12128  522 --LDELELQLFPQAgTLLHFLRKEAPDWEQSIGKVIS--PELLHRtdlDPEVWDGSVGGELNLYGVKLD---LKRIDVPE 594

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    836 LVNLEKDLVQQKDILKKEVQEEQEILECLKCEHDKESRLLEKHDESVTDVTevpQDFEKIKPVEYRLQYKERQLQYLLQN 915
Cdd:pfam12128  595 WAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFAR---TALKNARLDLRRLFDEKQSEKDKKNK 671

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    916 HLPTLLEEKQRAFEILDRGPLSLDNT----LYQVEKEMEEKEEQLAQY-----QANANQLQKLQATFE-FTANIARQEEK 985
Cdd:pfam12128  672 ALAERKDSANERLNSLEAQLKQLDKKhqawLEEQKEQKREARTEKQAYwqvveGALDAQLALLKAAIAaRRSGAKAELKA 751

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    986 VRKKEKEILESRE---------KQQREALERALARLE-RRHSALQRH------------------STLGMEIEEQRQKLA 1037
Cdd:pfam12128  752 LETWYKRDLASLGvdpdviaklKREIRTLERKIERIAvRRQEVLRYFdwyqetwlqrrprlatqlSNIERAISELQQQLA 831

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   1038 SLNSGSREQsglQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQKDhhgtleGKVASSSLPVSAEKSHLVPLMDar 1117
Cdd:pfam12128  832 RLIADTKLR---RAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKED------ANSEQAQGSIGERLAQLEDLKL-- 900

                          570       580
                   ....*....|....*....|.
gi 41327691   1118 INAYIEEEVQRRLQDLHRVIS 1138
Cdd:pfam12128  901 KRDYLSESVKKYVEHFKNVIA 921
COG5022 COG5022
Myosin heavy chain [General function prediction only];
600-856 4.47e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 44.68  E-value: 4.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  600 RQQREELekleskRKLIEEMEEKQKSDKAELERMQ-QEVETQRKETEIVQ-----LQIRKQEESLKRRSFHIENKLKDLL 673
Cdd:COG5022  806 LGSRKEY------RSYLACIIKLQKTIKREKKLREtEEVEFSLKAEVLIQkfgrsLKAKKRFSLLKKETIYLQSAQRVEL 879

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  674 AEKEKF-------------EEERLREQQEIELQKKRQE---EETFLRVqEELQRLKELNNNEKAEkfqifqELDQLQKEK 737
Cdd:COG5022  880 AERQLQelkidvksisslkLVNLELESEIIELKKSLSSdliENLEFKT-ELIARLKKLLNNIDLE------EGPSIEYVK 952

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  738 DEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRgEVQWVEEEKRDLEGIRESLLRVKEARAGGDedgeE 817
Cdd:COG5022  953 LPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKN-FKKELAELSKQYGALQESTKQLKELPVEVA----E 1027

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 41327691  818 LEKAQLRFFE--FKRRQLVKLVNLEKDLVQQKDILKKEVQE 856
Cdd:COG5022 1028 LQSASKIISSesTELSILKPLQKLKGLLLLENNQLQARYKA 1068
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 709-1080 4.49e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.73  E-value: 4.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    709 LQRLKELNNNEKAEKFQIFQElDQLQKEKDEQYAKLElEKKRLEEQEKEQVmlvAHLEEQ--LREKQEMIQLLRRGEVQW 786
Cdd:pfam17380  278 VQHQKAVSERQQQEKFEKMEQ-ERLRQEKEEKAREVE-RRRKLEEAEKARQ---AEMDRQaaIYAEQERMAMERERELER 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    787 V--EEEKRDLEGIRESLLRVKEARAggdedgEELEKAQLrffefKRRQLVKLVNLEKDLVQQKDILKKEVQEeqeilecl 864
Cdd:pfam17380  353 IrqEERKRELERIRQEEIAMEISRM------RELERLQM-----ERQQKNERVRQELEAARKVKILEEERQR-------- 413

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    865 kcehdkesrlleKHDESVTDVTEVPQDFEKIKPVEYRL--QYKERQLQYLLQNHLptlleEKQRAFEILdrgplsldntl 942
Cdd:pfam17380  414 ------------KIQQQKVEMEQIRAEQEEARQREVRRleEERAREMERVRLEEQ-----ERQQQVERL----------- 465

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    943 yqvekemeekeeqlaqyqananqlqklqatfeftaniaRQEEKVRKKEKEILESREKQQREALEralarlerrhsalQRH 1022
Cdd:pfam17380  466 --------------------------------------RQQEEERKRKKLELEKEKRDRKRAEE-------------QRR 494

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 41327691   1023 STLGMEIEEQRQKLAslnSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYE 1080
Cdd:pfam17380  495 KILEKELEERKQAMI---EEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEME 549
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 621-860 5.38e-04

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: 43.98  E-value: 5.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  621 EKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRrsfhIENKLkdllaekekfeeerlreqqeIELQKKRQEEE 700
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRI--------------------AALARRIRALE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  701 TFLRVQEelQRLKELNNNEkaekfqifQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLR 780
Cdd:COG4942   76 QELAALE--AELAELEKEI--------AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLA 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  781 RGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEI 860
Cdd:COG4942  146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
PRK12704 PRK12704
phosphodiesterase; Provisional
 665-809 6.79e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.00  E-value: 6.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   665 IENKLKDLLAEKEKfeeerlreqqeiELQKKRQEEEtfLRVQEELQRLKELNNNEKAEKFQIFQELDQ--LQKEK--DEQ 740
Cdd:PRK12704   36 AEEEAKRILEEAKK------------EAEAIKKEAL--LEAKEEIHKLRNEFEKELRERRNELQKLEKrlLQKEEnlDRK 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41327691   741 YAKLELEKKRLEEQEKEqvmlVAHLEEQLREKQEMIQLLrrgevqwVEEEKRDLEGIreSLLRVKEARA 809
Cdd:PRK12704  102 LELLEKREEELEKKEKE----LEQKQQELEKKEEELEEL-------IEEQLQELERI--SGLTAEEAKE 157
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 579-753 6.86e-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: 44.29  E-value: 6.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    579 LSKSRENLSAVMLynpglEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESL 658
Cdd:TIGR02169  831 LEKEIQELQEQRI-----DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    659 KRRSFHIEnKLKDLLAEKEKFEEERLREQQEIELQKKRQEE------------ETFLRVQEELQRLKELNNneKAEkfQI 726
Cdd:TIGR02169  906 EELEAQIE-KKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelsledvqAELQRVEEEIRALEPVNM--LAI--QE 980

                          170       180
                   ....*....|....*....|....*..
gi 41327691    727 FQELDQLQKEKDEQYAKLELEKKRLEE 753
Cdd:TIGR02169  981 YEEVLKRLDELKEKRAKLEEERKAILE 1007
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 692-897 8.35e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 43.45  E-value: 8.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    692 LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIF-QELDQLQKEKDEQYAKLELEKKRLEEQEKEqvmlvahLEEQLR 770
Cdd:pfam05262  183 VEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLkEELDKKQIDADKAQQKADFAQDNADKQRDE-------VRQKQQ 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    771 EKQemiQLLRRGEVQWVEEEKRDLEgiresllrvkearaggdEDGEELEKAQLrffEFKRrqlvKLVNLEKDLVQQKDIL 850
Cdd:pfam05262  256 EAK---NLPKPADTSSPKEDKQVAE-----------------NQKREIEKAQI---EIKK----NDEEALKAKDHKAFDL 308

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 41327691    851 KKEVQEEQEILEclkcehdkesrllEKHDESVTDVTEVPQDFEKIKP 897
Cdd:pfam05262  309 KQESKASEKEAE-------------DKELEAQKKREPVAEDLQKTKP 342
PX_RPK118_like cd07287
The phosphoinositide binding Phox Homology domain of RPK118-like proteins; The PX domain is a ...
 1216-1272 8.43e-04

The phosphoinositide binding Phox Homology domain of RPK118-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily bear similarity to human RPK118, which contains an N-terminal PX domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. It also binds the antioxidant peroxiredoxin-3 (PRDX3) and may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. Members of this subfamily also show similarity to sorting nexin 15 (SNX15), which contains PX and MIT domains but does not contain a kinase domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein.


Pssm-ID: 132820  Cd Length: 118  Bit Score: 40.72  E-value: 8.43e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41327691 1216 TVFRRYSRFREMHKTLKLKYAELAALE--FPP---KKLFGNKDERVIAERRSHLE---------------KYLRDFF 1272
Cdd:cd07287   39 VVWKRYSDFKKLHKDLWQIHKNLCRQSelFPPfakAKVFGRFDESVIEERRQCAEdllqfsanipalynsSQLEDFF 115
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
711-1089 9.53e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 9.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  711 RLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLE--EQLREKQEMIQLLRRGEVQWVE 788
Cdd:COG4717   64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAE 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  789 EEKRdLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKCEH 868
Cdd:COG4717  144 LPER-LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  869 DKesrlLEKHDESVTDVTEVPQDFEKIKPVEYRLQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKE 948
Cdd:COG4717  223 EE----LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKA 298

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  949 MEEKEEQLAQYQANANQLQKLQ-----ATFEFTANIARQEEKVRKKEKEILESREKQQREALERA-LARLERRHSALQRH 1022
Cdd:COG4717  299 SLGKEAEELQALPALEELEEEEleellAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqLEELEQEIAALLAE 378

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41327691 1023 STLGME--------IEEQRQKLASLNSGSREQsgLQASLEAEQEALEK-DQERLEYEIQQLKQKIYEVDGVQKDHH 1089
Cdd:COG4717  379 AGVEDEeelraaleQAEEYQELKEELEELEEQ--LEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELR 452
PX_p40phox cd06882
The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The ...
 1196-1273 1.08e-03

The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The PX domain is a phosphoinositide binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. p40phox contains an N-terminal PX domain, a central SH3 domain that binds p47phox, and a C-terminal PB1 domain that interacts with p67phox. It is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p40phox positively regulates NADPH oxidase in both phosphatidylinositol-3-phosphate (PI3P)-dependent and PI3P-independent manner. The PX domain is a phospholipid-binding module involved in the membrane targeting of proteins. The p40phox PX domain binds to PI3P, an abundant lipid in phagosomal membranes, playing an important role in the localization of NADPH oxidase. The PX domain of p40phox is also involved in protein-protein interaction.


Pssm-ID: 132792  Cd Length: 123  Bit Score: 40.50  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691 1196 QGKDAHFEFEVKITVLD-ETWTVFRRYSRFREMHKTLKLKY---AELAAL-----EFPPKKLFGNKDErvIAERR-SHLE 1265
Cdd:cd06882   15 RGFTNYYVFVIEVKTKGgSKYLIYRRYRQFFALQSKLEERFgpeAGSSAYdctlpTLPGKIYVGRKAE--IAERRiPLLN 92


                 ....*...
gi 41327691 1266 KYLRDFFS 1273
Cdd:cd06882   93 RYMKELLS 100
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 592-809 1.13e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 43.38  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   592 YNPGLEFERQQREELEKLESKrklIEEMEEKqksdKAELERMQQEVETQRKETEI-----VQLQIRKQEESLKRRSFHI- 665
Cdd:PRK05771   81 VKSLEELIKDVEEELEKIEKE---IKELEEE----ISELENEIKELEQEIERLEPwgnfdLDLSLLLGFKYVSVFVGTVp 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   666 ENKLKDLLAEKEKFEEERLREQQE----IELQKKRQEEEtflrVQEELQRLkELNNNEKAEKFQIFQELDQLQKEKDEQY 741
Cdd:PRK05771  154 EDKLEELKLESDVENVEYISTDKGyvyvVVVVLKELSDE----VEEELKKL-GFERLELEEEGTPSELIREIKEELEEIE 228

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41327691   742 AKLELEKKRLEEQEKEQVMLVAHLEEQL---REKQEM-IQLLRRGEV----QWVEEEkrDLEGIRESLLRVKEARA 809
Cdd:PRK05771  229 KERESLLEELKELAKKYLEELLALYEYLeieLERAEAlSKFLKTDKTfaieGWVPED--RVKKLKELIDKATGGSA 302
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
599-862 1.15e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  599 ERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKek 678
Cdd:COG4372   30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ-- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  679 feeerlreqqeielQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDE-----QYAKLELEKKRLEE 753
Cdd:COG4372  108 --------------EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEleeqlESLQEELAALEQEL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  754 QEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQL 833
Cdd:COG4372  174 QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLE 253

                        250       260
                 ....*....|....*....|....*....
gi 41327691  834 VKLVNLEKDLVQQKDILKKEVQEEQEILE 862
Cdd:COG4372  254 EVILKEIEELELAILVEKDTEEEELEIAA 282
PX_SNX15 cd07288
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; The PX domain is a ...
 1217-1269 1.17e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX15 contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. It plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein.


Pssm-ID: 132821  Cd Length: 118  Bit Score: 40.34  E-value: 1.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 41327691 1217 VFRRYSRFREMHKTLKLKYAEL--AALEFPP---KKLFGNKDERVIAERRSHLEKYLR 1269
Cdd:cd07288   40 VWKRYSDLKKLHGELAYTHRNLfrRQEEFPPfprAQVFGRFEAAVIEERRNAAEAMLL 97
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 597-702 1.25e-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: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  597 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEK 676
Cdd:COG4942  143 YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222

                         90       100
                 ....*....|....*....|....*.
gi 41327691  677 EKFEEERLREQQEIELQKKRQEEETF 702
Cdd:COG4942  223 EELEALIARLEAEAAAAAERTPAAGF 248
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 600-977 1.29e-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: 43.09  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    600 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQ------------EVETQRKETEIVQLQIRKQEESLKRrsfhIEN 667
Cdd:TIGR04523  267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNqkeqdwnkelksELKNQEKKLEEIQNQISQNNKIISQ----LNE 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    668 KLKDLlaEKEKFEEERLREQQEIELQKKRQEEETFLRVQEE-LQRLKELNNNEKAEKFQIfQELDQLQKEKDEQYAKLEL 746
Cdd:TIGR04523  343 QISQL--KKELTNSESENSEKQRELEEKQNEIEKLKKENQSyKQEIKNLESQINDLESKI-QNQEKLNQQKDEQIKKLQQ 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    747 EKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLrrgevqwvEEEKRDLEGIRESL-LRVKEARAGGDEDGEELEKAQlRF 825
Cdd:TIGR04523  420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVK--------ELIIKNLDNTRESLeTQLKVLSRSINKIKQNLEQKQ-KE 490

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    826 FEFKRRQLVKLVNLEKDLVQQKDILKKEVQE---EQEILECLKCEhdKESRLLEKHDESVTDVTEVpqDFEKIKPVeyrL 902
Cdd:TIGR04523  491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSlkeKIEKLESEKKE--KESKISDLEDELNKDDFEL--KKENLEKE---I 563

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41327691    903 QYKERQLQYLLQNHlpTLLEEKQRAFEILdrgplsldntlyqvekemeekeeqLAQYQANANQLQKLQATFEFTA 977
Cdd:TIGR04523  564 DEKNKEIEELKQTQ--KSLKKKQEEKQEL------------------------IDQKEKEKKDLIKEIEEKEKKI 612
FHA_RADIL cd22733
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...
 452-554 1.32e-03

forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein (Radil); Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438785  Cd Length: 113  Bit Score: 39.78  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  452 ELPHLIGIDDDLLSTGIILYHLKEGQTYVGRDDASTEQDIVLHGLDLESEHCIFENIGGT-------VTLIPLSGSQCSV 524
Cdd:cd22733    4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRRVRLPkhrseekLVLEPIPGAHVSV 83

                         90       100       110
                 ....*....|....*....|....*....|
gi 41327691  525 NGVQIVEATHLNQGAVILLGRTNMFRFNHP 554
Cdd:cd22733   84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 597-818 1.37e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.24  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    597 EFERQQREELEKLESKRKL-------IEEMEEKQKsdKAELERMQQEVETQRKETEIVQLQ-----IRKQEESLKRRSFH 664
Cdd:pfam01576  163 EFTSNLAEEEEKAKSLSKLknkheamISDLEERLK--KEEKGRQELEKAKRKLEGESTDLQeqiaeLQAQIAELRAQLAK 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    665 IENKLKDLLAEKEKFEEERLREqqeieLQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKE----KDEQ 740
Cdd:pfam01576  241 KEEELQAALARLEEETAQKNNA-----LKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEledtLDTT 315

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41327691    741 YAKLELEKKRleeqEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEARAGGDEDGEEL 818
Cdd:pfam01576  316 AAQQELRSKR----EQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAEL 389
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
 1182-1269 1.42e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX1, SNX2, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex.


Pssm-ID: 132769 [Multi-domain]  Cd Length: 114  Bit Score: 39.87  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691 1182 DPIKIsipryvlcGQGKDAHFEFEVKitvldeTWT-----------VFRRYSRFREMHKTLKLKYAELAALEFPPKKLFG 1250
Cdd:cd06859    7 DPVKV--------GDGMSAYVVYRVT------TKTnlpdfkksefsVLRRYSDFLWLYERLVEKYPGRIVPPPPEKQAVG 72

                         90       100
                 ....*....|....*....|.
gi 41327691 1251 NKDERV--IAERRSHLEKYLR 1269
Cdd:cd06859   73 RFKVKFefIEKRRAALERFLR 93
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
604-789 1.51e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   604 EELEKLESKRK-LIEEMEEKQKSDKAELERMQQEVETQRKETeIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEE 682
Cdd:PRK03918  563 KKLDELEEELAeLLKELEELGFESVEELEERLKELEPFYNEY-LELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   683 RLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEkfqiFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLV 762
Cdd:PRK03918  642 LEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAE----LEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717

                         170       180       190
                  ....*....|....*....|....*....|
gi 41327691   763 AHLE--EQLREK-QEMIQLLRRGEVQWVEE 789
Cdd:PRK03918  718 KALErvEELREKvKKYKALLKERALSKVGE 747
Caldesmon pfam02029
Caldesmon;
597-862 1.93e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.55  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    597 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRK----ETEIVQLQIRKQEESLKRRsfhienkLKDL 672
Cdd:pfam02029   10 ERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQggldEEEAFLDRTAKREERRQKR-------LQEA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    673 LAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLE 752
Cdd:pfam02029   83 LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDK 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    753 EQEKEQVMLVAHLEEQLRE---------KQEMIQLLRRGEV------QWVEEEKRDLEGIRESLLRVKEARAGGDEDGEE 817
Cdd:pfam02029  163 SEEAEEVPTENFAKEEVKDekikkekkvKYESKVFLDQKRGhpevksQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEV 242

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 41327691    818 LEKAQLRfFEFKRRQLVKLVNLEKDLVQQK--------DILKKEVQEEQEILE 862
Cdd:pfam02029  243 FLEAEQK-LEELRRRRQEKESEEFEKLRQKqqeaelelEELKKKREERRKLLE 294
PX_SNX16 cd07276
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ...
 1207-1263 2.25e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX16 contains a central PX domain followed by a coiled-coil region. SNX16 is localized in early and recycling endosomes through the binding of its PX domain to phosphatidylinositol-3-phosphate (PI3P). It plays a role in epidermal growth factor (EGF) signaling by regulating EGF receptor membrane trafficking.


Pssm-ID: 132809  Cd Length: 110  Bit Score: 38.93  E-value: 2.25e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691 1207 KITVL---DETWTVFRRYSRFREMHKTLKLKYAELaALEFPPKKLFGNKDERVIAERRSH 1263
Cdd:cd07276   24 KIRVEnkvGDSWFVFRRYTDFVRLNDKLKQMFPGF-RLSLPPKRWFKDNFDPDFLEERQL 82
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 596-858 2.84e-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: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 42.04  E-value: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    596 LEFERQQREELEKleSKRKLIEEMEEKQKSDKAELERMQQevetqRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAE 675
Cdd:pfam05557   43 LDRESDRNQELQK--RIRLLEKREAEAEEALREQAELNRL-----KKKYLEALNKKLNEKESQLADAREVISCLKNELSE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    676 kekfeeerlreqqeieLQKKRQEEETFLRVQE-ELQRLKELNNNEKA------EKFQIFQELDQLQKEKDEQYAKLELEk 748
Cdd:pfam05557  116 ----------------LRRQIQRAELELQSTNsELEELQERLDLLKAkaseaeQLRQNLEKQQSSLAEAEQRIKELEFE- 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    749 krLEEQE---------KEQVMLVAHLEEQLREKQEMIQLLR--RGEVQWVEEEKrdlEGIRESLLRVKEARAGGDEDGEE 817
Cdd:pfam05557  179 --IQSQEqdseivknsKSELARIPELEKELERLREHNKHLNenIENKLLLKEEV---EDLKRKLEREEKYREEAATLELE 253

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 41327691    818 LEKAQLRFFEFK----------------RRQLVKLVNLEKDLVQQKDILKKEVQEEQ 858
Cdd:pfam05557  254 KEKLEQELQSWVklaqdtglnlrspedlSRRIEQLQQREIVLKEENSSLTSSARQLE 310
PX_HS1BP3 cd06868
The phosphoinositide binding Phox Homology domain of HS1BP3; The PX domain is a ...
 1216-1282 2.87e-03

The phosphoinositide binding Phox Homology domain of HS1BP3; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Hematopoietic lineage cell-specific protein-1 (HS1) binding protein 3 (HS1BP3) associates with HS1 proteins through their SH3 domains, suggesting a role in mediating signaling. It has been reported that HS1BP3 might affect the IL-2 signaling pathway in hematopoietic lineage cells. Mutations in HS1BP3 may also be associated with familial Parkinson disease and essential tremor. HS1BP3 contains a PX domain, a leucine zipper, motifs similar to immunoreceptor tyrosine-based inhibitory motif and proline-rich regions. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.


Pssm-ID: 132778  Cd Length: 120  Bit Score: 38.93  E-value: 2.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41327691 1216 TVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFgnKDERVIAERRSHLEKYLRdFFSVMLQSATSP 1282
Cdd:cd06868   48 MVSKKYSEFEELYKKLSEKYPGTILPPLPRKALF--VSESDIRERRAAFNDFMR-FISKDEKLANCP 111
PRK12704 PRK12704
phosphodiesterase; Provisional
 613-777 2.94e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   613 RKLIEEMEEKQKSDKAELERmqqEVETQRKETEIVQlqirkQEESLKRRSfHIENKLKDLLAEkekfeeerlreQQEIEl 692
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEAKK---EAEAIKKEALLEA-----KEEIHKLRN-EFEKELRERRNE-----------LQKLE- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   693 QKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAKlelEKKRLEE-----QEKEQVMLVAHLEE 767
Cdd:PRK12704   89 KRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE---QLQELERisgltAEEAKEILLEKVEE 165

                         170
                  ....*....|.
gi 41327691   768 QLR-EKQEMIQ 777
Cdd:PRK12704  166 EARhEAAVLIK 176
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 600-678 3.10e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 3.10e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41327691  600 RQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSFHIENKLKDLLAEKEK 678
Cdd:COG3883  129 DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 695-1085 3.13e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.03  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    695 KRQEEETFLRVQEELQRLKELNNNEKAEKFQIFQEL----DQLQKEKDEQYAKLELEKKRLEEQE--KEQVMLVAH---- 764
Cdd:pfam15921   77 ERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVidlqTKLQEMQMERDAMADIRRRESQSQEdlRNQLQNTVHelea 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    765 ----LEEQLREKQEMIQLLRRgevqWVEEEKRDLEGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLE 840
Cdd:pfam15921  157 akclKEDMLEDSNTQIEQLRK----MMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTE 232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    841 KDLVQ--------QKDILKKEVQEEQEILecLKCEHDKESRLLEKHDESVTDVTE----VPQDFEKIKPVEYRLQYKERQ 908
Cdd:pfam15921  233 ISYLKgrifpvedQLEALKSESQNKIELL--LQQHQDRIEQLISEHEVEITGLTEkassARSQANSIQSQLEIIQEQARN 310

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    909 LQYLLQNHLPTL----------LEEKQRAFE----------ILDRGPLS---------------LDNTLYQVEKEMEEKE 953
Cdd:pfam15921  311 QNSMYMRQLSDLestvsqlrseLREAKRMYEdkieelekqlVLANSELTearterdqfsqesgnLDDQLQKLLADLHKRE 390

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    954 EQLAQYQANANQLQKLQATFEFTANIARQEEKVRKKEKEILESREKQQRE----ALERALARLERRHSALQRHSTLGMEI 1029
Cdd:pfam15921  391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQGKNESLEKVSSLTAQL 470

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41327691   1030 EEQRQKL-----------ASLNSGSREQSGLQASLEAEQEALE-------KDQERLEYEIQQLKQKIYEVDGVQ 1085
Cdd:pfam15921  471 ESTKEMLrkvveeltakkMTLESSERTVSDLTASLQEKERAIEatnaeitKLRSRVDLKLQELQHLKNEGDHLR 544
Caldesmon pfam02029
Caldesmon;
597-775 3.45e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.39  E-value: 3.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    597 EFERQQREELEKLESKRKLIEEMEeKQKSDKAELERMQQEVETQRKETEIVQLQIRKQEESLKRRSfhiENKLKDLLAEK 676
Cdd:pfam02029  147 TEVRQAEEEGEEEEDKSEEAEEVP-TENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQN---GEEEVTKLKVT 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    677 EKFEEERLREQQEIELQKKRQEEeTFLRVQEELQRLKELNNNE----KAEKFQIFQELDQLQKEKDEQYAKLELEKKRLE 752
Cdd:pfam02029  223 TKRRQGGLSQSQEREEEAEVFLE-AEQKLEELRRRRQEKESEEfeklRQKQQEAELELEELKKKREERRKLLEEEEQRRK 301

                          170       180
                   ....*....|....*....|...
gi 41327691    753 EQEKEQvmLVAHLEEQLREKQEM 775
Cdd:pfam02029  302 QEEAER--KLREEEEKRRMKEEI 322
PX_SNX14 cd06877
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ...
 1209-1270 3.70e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX14 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. It is expressed in the embryonic nervous system of mice, and is co-expressed in the motoneurons and the anterior pituary with Islet-1. SNX14 shows a similar domain architecture as SNX13, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.


Pssm-ID: 132787  Cd Length: 119  Bit Score: 38.51  E-value: 3.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41327691 1209 TVLDETWTVFRRYSRFRemhkTLKLKYAE----LAALEFPPKKLFGNKDERVIAERRSHLEKYLRD 1270
Cdd:cd06877   38 GHEPQHWSVLRRYNEFY----VLESKLTEfhgeFPDAPLPSRRIFGPKSYEFLESKREIFEEFLQK 99
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 604-757 3.75e-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: 41.54  E-value: 3.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    604 EELEKL-ESKRKLIEEMEEKQKSDKAELERMQQEVEtqRKETEIVQLQIRKQE-------------------ESLKRRSF 663
Cdd:TIGR04523  457 KNLDNTrESLETQLKVLSRSINKIKQNLEQKQKELK--SKEKELKKLNEEKKEleekvkdltkkisslkekiEKLESEKK 534

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    664 HIENKLKDLLAEKEKFEEERLREQQEIELQKKrqeeetflrvQEELQRLKELNNNEKAEKFQIFQELDQLQKEKDEQYAK 743
Cdd:TIGR04523  535 EKESKISDLEDELNKDDFELKKENLEKEIDEK----------NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE 604

                          170
                   ....*....|....
gi 41327691    744 LELEKKRLEEQEKE 757
Cdd:TIGR04523  605 IEEKEKKISSLEKE 618
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 746-1080 3.86e-03

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: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.42  E-value: 3.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    746 LEKKRLEEQEKEQVMLV--------AHLEEQLREKQEMIQLLRRGEVQwVEEEKRDLEGIRESL-LRVKEARAGGDEDGE 816
Cdd:pfam07888    9 LEEESHGEEGGTDMLLVvpraellqNRLEECLQERAELLQAQEAANRQ-REKEKERYKRDREQWeRQRRELESRVAELKE 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    817 ELEKAQLRFFEFKRRQlVKLVNLEKDLVQQKDILKKEVQE-EQEILEclkCEHDKESrLLEKHDESVTDVTEVPQDFEKI 895
Cdd:pfam07888   88 ELRQSREKHEELEEKY-KELSASSEELSEEKDALLAQRAAhEARIRE---LEEDIKT-LTQRVLERETELERMKERAKKA 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    896 KPVEYRLQYKERQLQYLLQ------NHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKEEQLAQYQANANQLQKL 969
Cdd:pfam07888  163 GAQRKEEEAERKQLQAKLQqteeelRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSL 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    970 QATFeftaNIARQEEKVRKKEKEILESREKQQREALERalARLERRHSALQRhSTLGMEIEEQRQKLAslnsgsREQSGL 1049
Cdd:pfam07888  243 QERL----NASERKVEGLGEELSSMAAQRDRTQAELHQ--ARLQAAQLTLQL-ADASLALREGRARWA------QERETL 309

                          330       340       350
                   ....*....|....*....|....*....|.
gi 41327691   1050 QASLEAEQEALEKdqerLEYEIQQLKQKIYE 1080
Cdd:pfam07888  310 QQSAEADKDRIEK----LSAELQRLEERLQE 336
PX_Vps5p cd06861
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ...
 1181-1270 4.00e-03

The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. The PX domain of Vps5p binds phosphatidylinositol-3-phosphate (PI3P). Similar to SNX1, Vps5p contains a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1.


Pssm-ID: 132771  Cd Length: 112  Bit Score: 38.49  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691 1181 KDPIKIsipryvlcGQGKDAHFEFEV--KITVLD---ETWTVFRRYSRFREMHKTLKLKYAELAALEFPPKKLFGNKDER 1255
Cdd:cd06861    6 GDPHKV--------GDLTSAHTVYTVrtRTTSPNfevSSFSVLRRYRDFRWLYRQLQNNHPGVIVPPPPEKQSVGRFDDN 77

                         90
                 ....*....|....*
gi 41327691 1256 VIAERRSHLEKYLRD 1270
Cdd:cd06861   78 FVEQRRAALEKMLRK 92
46 PHA02562
endonuclease subunit; Provisional
 607-850 4.41e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   607 EKLESKRKLIEEMEEKQKSDKAELERMqqeVETQRKETEivqlQIRKQEESLKRRSFHIENKLKDLLAEKEKFEEERLRE 686
Cdd:PHA02562  195 QQIKTYNKNIEEQRKKNGENIARKQNK---YDELVEEAK----TIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKI 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   687 QQEIELQKKrqeEETFLRVQEE----LQRLKElnNNEKAEKfqIFQELDQLQKekdeqyaKLELEKKRLEEQEKeqvmlv 762
Cdd:PHA02562  268 KSKIEQFQK---VIKMYEKGGVcptcTQQISE--GPDRITK--IKDKLKELQH-------SLEKLDTAIDELEE------ 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   763 ahLEEQLREKQEMIQLLRRGevqwVEEEKRDLEGIRESLLRVK----EARAGGDEDGEELEKAQlrffefkrRQLVKLVN 838
Cdd:PHA02562  328 --IMDEFNEQSKKLLELKNK----ISTNKQSLITLVDKAKKVKaaieELQAEFVDNAEELAKLQ--------DELDKIVK 393

                         250
                  ....*....|..
gi 41327691   839 LEKDLVQQKDIL 850
Cdd:PHA02562  394 TKSELVKEKYHR 405
Caldesmon pfam02029
Caldesmon;
610-761 4.50e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.01  E-value: 4.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    610 ESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEiVQLQIRKQEESLKRRSFHIENklkdllAEKEKFEEERLREQQE 689
Cdd:pfam02029  206 EVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE-VFLEAEQKLEELRRRRQEKES------EEFEKLRQKQQEAELE 278

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41327691    690 IELQKKRQEEETFLRVQEELQRlkelnNNEKAEKfqifqeldQLQKEKDEQYAKLELEKKRLEEQEKEQVML 761
Cdd:pfam02029  279 LEELKKKREERRKLLEEEEQRR-----KQEEAER--------KLREEEEKRRMKEEIERRRAEAAEKRQKLP 337
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 555-1139 4.53e-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: 41.50  E-value: 4.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    555 KEAAKLREKRKSGLLSSFSLSMTDLSKSRENLSAVMLYNPGLEFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQ 634
Cdd:pfam02463  422 KEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK 501

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    635 QEVETQRKETEIVQLQIRKqeeslKRRSFHIENKLKDLLAEKEKFEEERLREQQEIELQKKRQEEETFLRVQEELQRLKE 714
Cdd:pfam02463  502 ESKARSGLKVLLALIKDGV-----GGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLG 576

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    715 LNNNEKAEKFQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEEQLREKQEMIQLLRRGEVQWVEEEKRDL 794
Cdd:pfam02463  577 ARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEE 656

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    795 EGIRESLLRVKEARAGGDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKEVQEEQEILECLKceHDKESRL 874
Cdd:pfam02463  657 GLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRV--QEAQDKI 734

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    875 LEKHDESVTDVTEVPQDFEKIKP-VEYRLQYKERQLQYLLQNHLPTLLEEKQRAFEILDRGPLSLDNTLYQVEKEMEEKE 953
Cdd:pfam02463  735 NEELKLLKQKIDEEEEEEEKSRLkKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEA 814

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    954 EQLAQYQANANQLQKlqatfeftaniaRQEEKVRKKEKEILE------SREKQQREALERALARLERRHSALQRHSTL-- 1025
Cdd:pfam02463  815 ELLEEEQLLIEQEEK------------IKEEELEELALELKEeqklekLAEEELERLEEEITKEELLQELLLKEEELEeq 882

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   1026 -------GMEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKIYEVDGVQKDHHGTLEGKVAS 1098
Cdd:pfam02463  883 klkdeleSKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERN 962

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|.
gi 41327691   1099 SSLPVSAEKSHLVPLMDARINAYIEEEVQRRLQDLHRVISE 1139
Cdd:pfam02463  963 KRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 584-758 4.64e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   584 ENLSAVMLyNPGLEFERQQREELEKLESKRKliEEMEEKQKSDKAELERMQQEVETQR-----KETEIVQLQIRKQEESL 658
Cdd:PRK09510   48 SVIDAVMV-DPGAVVEQYNRQQQQQKSAKRA--EEQRKKKEQQQAEELQQKQAAEQERlkqleKERLAAQEQKKQAEEAA 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691   659 KrrsfhienklkdLLAEKEKfeeerlreqqEIELQKKRQEEETFLRVQEELQRLKELNNNEKAEKfQIFQELDQLQKEKD 738
Cdd:PRK09510  125 K------------QAALKQK----------QAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEA-KKKAEAEAAKKAAA 181

                         170       180
                  ....*....|....*....|
gi 41327691   739 EQYAKLELEKKRLEEQEKEQ 758
Cdd:PRK09510  182 EAKKKAEAEAAAKAAAEAKK 201
PX_SNX21 cd07301
The phosphoinositide binding Phox Homology domain of Sorting Nexin 21; The PX domain is a ...
 1219-1274 4.89e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 21; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.


Pssm-ID: 132834  Cd Length: 112  Bit Score: 38.25  E-value: 4.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41327691 1219 RRYSRFREMHKTLKLKY-AELAALEFPPKKLFGNKDERVIAERRSHLEKYLRDFFSV 1274
Cdd:cd07301   40 RRYSDFERLHRRLRRLFgGEMAGVSFPRKRLRKNFTAETIAKRSRAFEQFLCHLHSL 96
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 597-884 5.04e-03

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: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.03  E-value: 5.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    597 EFERQQREELEKLESKRKLIEEMEEKQKSDKAELERMQQEVETQRKETEIVQLQIRKQE-----------------ESLK 659
Cdd:pfam07888   77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEediktltqrvleretelERMK 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    660 RRSFHIENKLKDLLAEKEKFEEERLREQQEI-----ELQKKR----QEEETFLRVQEELQRLKELNNN---EKAEKFQIF 727
Cdd:pfam07888  157 ERAKKAGAQRKEEEAERKQLQAKLQQTEEELrslskEFQELRnslaQRDTQVLQLQDTITTLTQKLTTahrKEAENEALL 236

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    728 QELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHLEE-QLREKQEMIQL------LRRGEVQW----------VEEE 790
Cdd:pfam07888  237 EELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQaRLQAAQLTLQLadaslaLREGRARWaqeretlqqsAEAD 316

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    791 KRDLEGIRESLLRVKEARaggDEDGEELEKAQLRFFEFKRRQLVKLVNLEKDLVQQKDILKKeVQEEQEILECLKCEHDK 870
Cdd:pfam07888  317 KDRIEKLSAELQRLEERL---QEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRV-AQKEKEQLQAEKQELLE 392

                          330
                   ....*....|....
gi 41327691    871 ESRLLEKHDESVTD 884
Cdd:pfam07888  393 YIRQLEQRLETVAD 406
RNase_Y_N pfam12072
RNase Y N-terminal region;
612-757 5.89e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 39.48  E-value: 5.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    612 KRKLIEEMEEKQKSdKAELERmqqEVETQRKETEIVQLQIRKQEESLKRRSFHIENKlKDLLAEKEKfeeerlrEQQEIE 691
Cdd:pfam12072   52 KEALLEAKEEIHKL-RAEAER---ELKERRNELQRQERRLLQKEETLDRKDESLEKK-EESLEKKEK-------ELEAQQ 119

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41327691    692 LQKKRQEEETFLRVQEELQRLKELNNNEKAEKFQIFqeLDQLQKEKDEQYAKL--ELEKKRLEEQEKE 757
Cdd:pfam12072  120 QQLEEKEEELEELIEEQRQELERISGLTSEEAKEIL--LDEVEEELRHEAAVMikEIEEEAKEEADKK 185
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 607-807 6.52e-03

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: 40.25  E-value: 6.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  607 EKLESKRKLIEEMEEKqksdKAELERMQQEVETQRKETEIVQLqIRKQEESLKRRSFHIENKLKDLLAEKEKFeeerlre 686
Cdd:cd16269   87 EDQKFQKKLMEQLEEK----KEEFCKQNEEASSKRCQALLQEL-SAPLEEKISQGSYSVPGGYQLYLEDREKL------- 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  687 qqeieLQKKRQEEETFLRVQEELQR-LKELNNNEKAEKfQIFQELDQLQKEKDEQYAKLELEKKRLEEQEKEQVMLVAHL 765
Cdd:cd16269  155 -----VEKYRQVPRKGVKAEEVLQEfLQSKEAEAEAIL-QADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKL 228

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 41327691  766 EEQLREKQEMIQLLRRGEVQWVEEEKRDLEGIRESLLRVKEA 807
Cdd:cd16269  229 EDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEA 270
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 599-753 7.20e-03

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.48  E-value: 7.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    599 ERQQREELEKLESKRKLIEEMEEkqksdKAELERMQQEVETQRKETEivqlqiRKQEESLKRRsfhienklkdlLAEKEK 678
Cdd:pfam05672   28 EREEQERLEKEEEERLRKEELRR-----RAEEERARREEEARRLEEE------RRREEEERQR-----------KAEEEA 85

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41327691    679 FEEERLREQQEIELQKKRQEEETFLRVQEELQRLkelnnnekaEKFQIFQELDQLQKEKdeqyakleleKKRLEE 753
Cdd:pfam05672   86 EEREQREQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER----------KKRIEE 141
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 600-716 8.84e-03

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: 40.51  E-value: 8.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691    600 RQQREELEKLEskRKLIEEMEEKQKSDKAELERMQQ-EVETQRKETE-IVQLQIRKQEESlkrrsfhIENKLKDLLAEKE 677
Cdd:pfam09731  319 EKQKEELDKLA--EELSARLEEVRAADEAQLRLEFErEREEIRESYEeKLRTELERQAEA-------HEEHLKDVLVEQE 389

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 41327691    678 kfeeerlreqqeIELQKKRQEEETFLRVQEELQRLKELN 716
Cdd:pfam09731  390 ------------IELQREFLQDIKEKVEEERAGRLLKLN 416
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 999-1108 9.31e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 9.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327691  999 KQQREALERALARLERRHSALQRhstlgmEIEEQRQKLASLNSGSREQSGLQASLEAEQEALEKDQERLEYEIQQLKQKI 1078
Cdd:COG3883  139 KADKAELEAKKAELEAKLAELEA------LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212

                         90       100       110
                 ....*....|....*....|....*....|
gi 41327691 1079 YEVDGVQKDHHGTLEGKVASSSLPVSAEKS 1108
Cdd:COG3883  213 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
 
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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