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Conserved domains on  [gi|74272287|ref|NP_004985|]
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matrix metalloproteinase-9 preproprotein [Homo sapiens]

Protein Classification

ZnMc_MMP and HX domain-containing protein( domain architecture ID 11995254)

protein containing domains ZnMc_MMP, FN2, PT, and HX

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 514-704 5.57e-65

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


:

Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 213.33  E-value: 5.57e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287 514 DACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGrgSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGA 593
Cdd:cd00094   2 DACDPLSFDAVTTLRGELYFFKGRYFWRLSPG--KPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287 594 SV--LGPRRLDKLGLGADVAQVTGALRSG-RGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYR-E 669
Cdd:cd00094  80 NLepGYPKPISDLGFPPTVKQIDAALRWPdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 74272287 670 KAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQC 704
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 115-444 3.19e-61

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


:

Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 202.08  E-value: 3.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287   115 KWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPP 194
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287   195 GPGIQGDAHFDDDELWSLGKGvvvptrfgnadgaachfpfifegrsysacttdgrsdglpwcsttanydtddrfgfcpse 274
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287   275 rlytqdgnadgkpcqfpfifqgqsysacttdgrsdgyrwcattanydrdklfgfcptradstvmggnsagelcvfpftfl 354
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287   355 gkeystctsegrgdgrlwcattsnfdsdkkwgfcPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGP--PLH 432
Cdd:pfam00413 102 ----------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKkfRLS 147

                         330
                  ....*....|..
gi 74272287   433 KDDVNGIRHLYG 444
Cdd:pfam00413 148 QDDIKGIQQLYG 159
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 281-329 1.81e-22

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


:

Pssm-ID: 128373  Cd Length: 49  Bit Score: 90.82  E-value: 1.81e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 74272287    281 GNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFC 329
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 223-271 4.10e-22

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


:

Pssm-ID: 128373  Cd Length: 49  Bit Score: 89.67  E-value: 4.10e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 74272287    223 GNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFC 271
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 340-388 1.75e-21

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


:

Pssm-ID: 128373  Cd Length: 49  Bit Score: 87.74  E-value: 1.75e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 74272287    340 GNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFC 388
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
PT pfam04886
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a ...
 472-506 7.83e-11

PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat.


:

Pssm-ID: 282710 [Multi-domain]  Cd Length: 36  Bit Score: 57.10  E-value: 7.83e-11
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 74272287   472 PPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATT 506
Cdd:pfam04886   1 QPTAQPTAQPTVQPTGQPTAQPTDQPTAQPTDAPT 35
 
Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 514-704 5.57e-65

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 213.33  E-value: 5.57e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287 514 DACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGrgSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGA 593
Cdd:cd00094   2 DACDPLSFDAVTTLRGELYFFKGRYFWRLSPG--KPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287 594 SV--LGPRRLDKLGLGADVAQVTGALRSG-RGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYR-E 669
Cdd:cd00094  80 NLepGYPKPISDLGFPPTVKQIDAALRWPdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 74272287 670 KAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQC 704
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 115-444 3.19e-61

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 202.08  E-value: 3.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287   115 KWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPP 194
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287   195 GPGIQGDAHFDDDELWSLGKGvvvptrfgnadgaachfpfifegrsysacttdgrsdglpwcsttanydtddrfgfcpse 274
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287   275 rlytqdgnadgkpcqfpfifqgqsysacttdgrsdgyrwcattanydrdklfgfcptradstvmggnsagelcvfpftfl 354
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287   355 gkeystctsegrgdgrlwcattsnfdsdkkwgfcPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGP--PLH 432
Cdd:pfam00413 102 ----------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKkfRLS 147

                         330
                  ....*....|..
gi 74272287   433 KDDVNGIRHLYG 444
Cdd:pfam00413 148 QDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 115-444 4.28e-52

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 177.40  E-value: 4.28e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287 115 KWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYS-RDADIVIQFGVAEHGDGYPFDGKDGLLAHAFP 193
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSgQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287 194 PGpGIQGDAHFDDDELWSLGKGvvvptrfgnadgaachfpfifegrsysacttdgrsdglpwcsttanydtddrfgfcps 273
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSD---------------------------------------------------------- 101

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287 274 erlytqdgnadgkpcqfpfifqgqsysacttdgrsdgyrwcattanydrdklfgfcptradstvmggnsagelcvfpftf 353
Cdd:cd04278     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287 354 lgkeystctsegrgdgrlwcattsnfdsdkkwgfcpDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPP-LH 432
Cdd:cd04278 102 ------------------------------------SGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFkLS 145

                       330
                ....*....|..
gi 74272287 433 KDDVNGIRHLYG 444
Cdd:cd04278 146 QDDIRGIQALYG 157
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 281-329 1.81e-22

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


Pssm-ID: 128373  Cd Length: 49  Bit Score: 90.82  E-value: 1.81e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 74272287    281 GNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFC 329
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 223-271 4.10e-22

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


Pssm-ID: 128373  Cd Length: 49  Bit Score: 89.67  E-value: 4.10e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 74272287    223 GNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFC 271
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 340-388 1.75e-21

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


Pssm-ID: 128373  Cd Length: 49  Bit Score: 87.74  E-value: 1.75e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 74272287    340 GNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFC 388
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 282-329 4.42e-21

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.


Pssm-ID: 238019  Cd Length: 48  Bit Score: 86.59  E-value: 4.42e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 74272287 282 NADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFC 329
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 224-271 4.96e-21

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.


Pssm-ID: 238019  Cd Length: 48  Bit Score: 86.59  E-value: 4.96e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 74272287 224 NADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFC 271
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
347-388 9.99e-21

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 85.31  E-value: 9.99e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 74272287   347 CVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFC 388
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 341-388 7.89e-20

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.


Pssm-ID: 238019  Cd Length: 48  Bit Score: 83.12  E-value: 7.89e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 74272287 341 NSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFC 388
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
230-271 4.05e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 81.08  E-value: 4.05e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 74272287   230 CHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFC 271
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
288-329 9.45e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.92  E-value: 9.45e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 74272287   288 CQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFC 329
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 112-218 1.16e-16

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 77.01  E-value: 1.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287    112 GDLKWHHHNITYWIqnYSEDLPRAViDDAFARAFALWSAVTPLTFTRVYSrDADIVIQFGVaehGDGYPFdgkdglLAHA 191
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERTG-TADIYISFGS---GDSGCT------LSHA 67

                           90       100
                   ....*....|....*....|....*..
gi 74272287    192 FPPGpgiqGDAHFdDDELWSLGKGVVV 218
Cdd:smart00235  68 GRPG----GDQHL-SLGNGCINTGVAA 89
PT pfam04886
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a ...
 472-506 7.83e-11

PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat.


Pssm-ID: 282710 [Multi-domain]  Cd Length: 36  Bit Score: 57.10  E-value: 7.83e-11
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 74272287   472 PPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATT 506
Cdd:pfam04886   1 QPTAQPTAQPTVQPTGQPTAQPTDQPTAQPTDAPT 35
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 521-565 2.26e-07

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 47.62  E-value: 2.26e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 74272287    521 FDAIAEIGN-QLYLFKDGKYWRFSEGRGsRPQGPFLIADKWPALPR 565
Cdd:smart00120   1 IDAAFELRDgKTYFFKGDKYWRFDPKRV-DPGYPKLISSFFPGLPC 45
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 389-443 8.08e-06

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 47.76  E-value: 8.08e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 74272287 389 PDQ-GYSLFLVAAHEFGHALGL-DHSSVPEALMYP-MYRftEGPPLHKDDVNGIRHLY 443
Cdd:COG5549 175 PNQtGKYLLATARHELGHALGIwGHSPSPTDAMYFsQVR--NPPPISPRDINTLKRIY 230
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 521-564 1.89e-05

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 42.17  E-value: 1.89e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 74272287   521 FDAIAEIG-NQLYLFKDGKYWRFSEGRgSRPQGPFLIADkWPALP 564
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQR-VEPGYPKLISD-FPGLP 43
 
Name Accession Description Interval E-value
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 514-704 5.57e-65

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 213.33  E-value: 5.57e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287 514 DACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGrgSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGA 593
Cdd:cd00094   2 DACDPLSFDAVTTLRGELYFFKGRYFWRLSPG--KPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287 594 SV--LGPRRLDKLGLGADVAQVTGALRSG-RGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYR-E 669
Cdd:cd00094  80 NLepGYPKPISDLGFPPTVKQIDAALRWPdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 74272287 670 KAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQC 704
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 115-444 3.19e-61

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 202.08  E-value: 3.19e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287   115 KWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPP 194
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287   195 GPGIQGDAHFDDDELWSLGKGvvvptrfgnadgaachfpfifegrsysacttdgrsdglpwcsttanydtddrfgfcpse 274
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSD----------------------------------------------------------- 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287   275 rlytqdgnadgkpcqfpfifqgqsysacttdgrsdgyrwcattanydrdklfgfcptradstvmggnsagelcvfpftfl 354
Cdd:pfam00413     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287   355 gkeystctsegrgdgrlwcattsnfdsdkkwgfcPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGP--PLH 432
Cdd:pfam00413 102 ----------------------------------PPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKkfRLS 147

                         330
                  ....*....|..
gi 74272287   433 KDDVNGIRHLYG 444
Cdd:pfam00413 148 QDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 115-444 4.28e-52

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 177.40  E-value: 4.28e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287 115 KWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYS-RDADIVIQFGVAEHGDGYPFDGKDGLLAHAFP 193
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSgQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287 194 PGpGIQGDAHFDDDELWSLGKGvvvptrfgnadgaachfpfifegrsysacttdgrsdglpwcsttanydtddrfgfcps 273
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSD---------------------------------------------------------- 101

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287 274 erlytqdgnadgkpcqfpfifqgqsysacttdgrsdgyrwcattanydrdklfgfcptradstvmggnsagelcvfpftf 353
Cdd:cd04278     --------------------------------------------------------------------------------

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287 354 lgkeystctsegrgdgrlwcattsnfdsdkkwgfcpDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPP-LH 432
Cdd:cd04278 102 ------------------------------------SGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFkLS 145

                       330
                ....*....|..
gi 74272287 433 KDDVNGIRHLYG 444
Cdd:cd04278 146 QDDIRGIQALYG 157
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 281-329 1.81e-22

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


Pssm-ID: 128373  Cd Length: 49  Bit Score: 90.82  E-value: 1.81e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 74272287    281 GNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFC 329
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 223-271 4.10e-22

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


Pssm-ID: 128373  Cd Length: 49  Bit Score: 89.67  E-value: 4.10e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 74272287    223 GNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFC 271
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 340-388 1.75e-21

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


Pssm-ID: 128373  Cd Length: 49  Bit Score: 87.74  E-value: 1.75e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 74272287    340 GNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFC 388
Cdd:smart00059   1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 282-329 4.42e-21

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.


Pssm-ID: 238019  Cd Length: 48  Bit Score: 86.59  E-value: 4.42e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 74272287 282 NADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFC 329
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 224-271 4.96e-21

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.


Pssm-ID: 238019  Cd Length: 48  Bit Score: 86.59  E-value: 4.96e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 74272287 224 NADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFC 271
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
347-388 9.99e-21

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 85.31  E-value: 9.99e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 74272287   347 CVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFC 388
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 341-388 7.89e-20

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.


Pssm-ID: 238019  Cd Length: 48  Bit Score: 83.12  E-value: 7.89e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 74272287 341 NSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFC 388
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
230-271 4.05e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 81.08  E-value: 4.05e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 74272287   230 CHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFC 271
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
fn2 pfam00040
Fibronectin type II domain;
288-329 9.45e-19

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 79.92  E-value: 9.45e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 74272287   288 CQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFC 329
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 112-218 1.16e-16

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 77.01  E-value: 1.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287    112 GDLKWHHHNITYWIqnYSEDLPRAViDDAFARAFALWSAVTPLTFTRVYSrDADIVIQFGVaehGDGYPFdgkdglLAHA 191
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERTG-TADIYISFGS---GDSGCT------LSHA 67

                           90       100
                   ....*....|....*....|....*..
gi 74272287    192 FPPGpgiqGDAHFdDDELWSLGKGVVV 218
Cdd:smart00235  68 GRPG----GDQHL-SLGNGCINTGVAA 89
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 382-444 1.08e-12

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 66.33  E-value: 1.08e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74272287 382 DKKWGFCPDQG-YSLFLVAAHEFGHALGLDHSSV-PEALMYPMY--RFTEGPPLHKDDVNGIRHLYG 444
Cdd:cd04279  90 DINLGPGQPRGaENLQAIALHELGHALGLWHHSDrPEDAMYPSQgqGPDGNPTLSARDVATLKRLYG 156
PT pfam04886
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a ...
 472-506 7.83e-11

PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat.


Pssm-ID: 282710 [Multi-domain]  Cd Length: 36  Bit Score: 57.10  E-value: 7.83e-11
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 74272287   472 PPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATT 506
Cdd:pfam04886   1 QPTAQPTAQPTVQPTGQPTAQPTDQPTAQPTDAPT 35
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 398-444 6.72e-10

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 57.75  E-value: 6.72e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 74272287    398 VAAHEFGHALGLDHSSVPEA---LMYPMYRF--TEGPPLHKDDVNGIRHLYG 444
Cdd:smart00235  87 VAAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLGIPYDYG 138
PT pfam04886
PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a ...
 469-499 4.36e-09

PT repeat; This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat.


Pssm-ID: 282710 [Multi-domain]  Cd Length: 36  Bit Score: 52.48  E-value: 4.36e-09
                          10        20        30
                  ....*....|....*....|....*....|.
gi 74272287   469 PTGPPTVHPSERPTAGPTGPPSAGPTGPPTA 499
Cdd:pfam04886   6 PTAQPTVQPTGQPTAQPTDQPTAQPTDAPTA 36
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 521-565 2.26e-07

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 47.62  E-value: 2.26e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 74272287    521 FDAIAEIGN-QLYLFKDGKYWRFSEGRGsRPQGPFLIADKWPALPR 565
Cdd:smart00120   1 IDAAFELRDgKTYFFKGDKYWRFDPKRV-DPGYPKLISSFFPGLPC 45
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 389-443 8.08e-06

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 47.76  E-value: 8.08e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 74272287 389 PDQ-GYSLFLVAAHEFGHALGL-DHSSVPEALMYP-MYRftEGPPLHKDDVNGIRHLY 443
Cdd:COG5549 175 PNQtGKYLLATARHELGHALGIwGHSPSPTDAMYFsQVR--NPPPISPRDINTLKRIY 230
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 521-564 1.89e-05

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 42.17  E-value: 1.89e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 74272287   521 FDAIAEIG-NQLYLFKDGKYWRFSEGRgSRPQGPFLIADkWPALP 564
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQR-VEPGYPKLISD-FPGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 613-658 1.89e-04

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 39.53  E-value: 1.89e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 74272287    613 VTGALRSGRGKMLLFSGRRLWRFDVKAqmVDPRSASEVDRMFPGVP 658
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLP 44
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 333-444 5.74e-04

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 41.63  E-value: 5.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74272287 333 ADSTVMGGNSAGeLCVFPFTflgkeystcTSEGRGDGRLWcattsnFDSDKKWGFCPDQGYSlFLVAAHEFGHALGLDHS 412
Cdd:cd04277  68 GNSSDPDGNTAG-YAYYPGS---------GSGTAYGGDIW------FNSSYDTNSDSPGSYG-YQTIIHEIGHALGLEHP 130

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 74272287 413 -----SVPEALMYP--------M-YRFTEGPPLHKD----------DVNGIRHLYG 444
Cdd:cd04277 131 gdyngGDPVPPTYAldsreytvMsYNSGYGNGASAGggypqtpmllDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 392-443 8.75e-04

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 40.58  E-value: 8.75e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74272287 392 GYSLFLVAAHEFGHALGLDHSSVPEA--------------------LMYPMY-RFTEG--PPLHKDDVNGIRHLY 443
Cdd:cd00203  93 TKEGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKgSFSDGqrKDFSQCDIDQINKLY 167
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 613-658 8.84e-04

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 37.55  E-value: 8.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 74272287   613 VTGALRSGRGKMLLFSGRRLWRFDV-KAQMVDPRSASEvdrmFPGVP 658
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPqRVEPGYPKLISD----FPGLP 43
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 398-443 9.27e-04

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 40.56  E-value: 9.27e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74272287 398 VAAHEFGHALGLDHSS----------------VPEALMYPMYR-------FTEGPPLHKDDVNGIRHLY 443
Cdd:cd04268  97 TAEHELGHALGLRHNFaasdrddnvdllaekgDTSSVMDYAPSnfsiqlgDGQKYTIGPYDIAAIKKLY 165
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 139-207 1.14e-03

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 40.48  E-value: 1.14e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74272287 139 DAFARAFALWSAVTPLTFTRV-YSRDADIVIQFGVAEHGDGYpfdgkdgllAHAFPPGPGI----QGDAHFDDD 207
Cdd:cd04277  37 AAARDALEAWEDVADIDFVEVsDNSGADIRFGNSSDPDGNTA---------GYAYYPGSGSgtayGGDIWFNSS 101
 
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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