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Conserved domains on  [gi|1958677271|ref|XP_038948379|]
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EMI domain-containing protein 1 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 34-101 2.56e-19

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


:

Pssm-ID: 462204  Cd Length: 69  Bit Score: 81.70  E-value: 2.56e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958677271  34 RNWCSYvvtRTVSCHVQNGT--YLQRV----LQSCPWPVGCPgnSYRTVVRPMYKVMYKTVTAREWRCCPGHSG 101
Cdd:pfam07546   1 RNVCAY---KVVSCVVVTGTesYVQPVykpyLTWCAGHRRCS--TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 321-370 1.92e-11

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


:

Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 59.04  E-value: 1.92e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958677271 321 GHMGTPGPSGPKGTSGPPGEKGERGLPGEPGPQGLMGFPGEPGPKGDPGE 370
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 189-376 5.38e-04

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 42.20  E-value: 5.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677271 189 DGGLQDRVDSWEL--PGPTGPKGDTDRQDPirirgppgpQGPPGRPGQTGAAGTPGKMGPPGPPGPPGPPGPPAPVGPPS 266
Cdd:NF038329  107 DEGLQQLKGDGEKgePGPAGPAGPAGEQGP---------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677271 267 AQvslhGDPLLSNTFTEMGSHWPQGPTGPPGPPGPPGPMGPPGLPGPTGAPGSPGHMG--TPGPSGPKGTSGPPGEKGER 344
Cdd:NF038329  178 KD----GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPD 253

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958677271 345 GLPGEPGPQGLMGFPGEPGPKGDPGEKSHWGE 376
Cdd:NF038329  254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285
 
Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 34-101 2.56e-19

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


Pssm-ID: 462204  Cd Length: 69  Bit Score: 81.70  E-value: 2.56e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958677271  34 RNWCSYvvtRTVSCHVQNGT--YLQRV----LQSCPWPVGCPgnSYRTVVRPMYKVMYKTVTAREWRCCPGHSG 101
Cdd:pfam07546   1 RNVCAY---KVVSCVVVTGTesYVQPVykpyLTWCAGHRRCS--TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 321-370 1.92e-11

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 59.04  E-value: 1.92e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958677271 321 GHMGTPGPSGPKGTSGPPGEKGERGLPGEPGPQGLMGFPGEPGPKGDPGE 370
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 321-369 2.33e-07

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 52.60  E-value: 2.33e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958677271 321 GHMGTPGPSGPKGTSGPPGEKGERGLPGEPGPQGLMGFPGEPGPKGDPG 369
Cdd:NF038329  239 GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 297-376 4.23e-07

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 51.83  E-value: 4.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677271 297 GPPGPPGPMGPPGLPGPTGAPGSPGHMGTPGPSGPKGTSGPPGEKGERGLPGEPGPQGLMGFPGEPGPKGDPGEKSHWGE 376
Cdd:NF038329  147 GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 300-377 6.36e-05

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 44.90  E-value: 6.36e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958677271 300 GPPGPMGPpglpgptgapgsPGHMGTPGPSGPKGTSGPPGEKGERGLPGEPGPQGLMGFPGEPGPKGDPGEKSHWGEG 377
Cdd:NF038329  168 GEAGPQGP------------AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG 233
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 189-376 5.38e-04

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 42.20  E-value: 5.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677271 189 DGGLQDRVDSWEL--PGPTGPKGDTDRQDPirirgppgpQGPPGRPGQTGAAGTPGKMGPPGPPGPPGPPGPPAPVGPPS 266
Cdd:NF038329  107 DEGLQQLKGDGEKgePGPAGPAGPAGEQGP---------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677271 267 AQvslhGDPLLSNTFTEMGSHWPQGPTGPPGPPGPPGPMGPPGLPGPTGAPGSPGHMG--TPGPSGPKGTSGPPGEKGER 344
Cdd:NF038329  178 KD----GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPD 253

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958677271 345 GLPGEPGPQGLMGFPGEPGPKGDPGEKSHWGE 376
Cdd:NF038329  254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-370 6.88e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 38.73  E-value: 6.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958677271 305 MGPPGLPGPTGAPGSPGHMGTPGPSGPKGTSGPPGEKGERGLPGEPGPQGLMGFPGEPGPKGDPGE 370
Cdd:NF038329  253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK 318
 
Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
 34-101 2.56e-19

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


Pssm-ID: 462204  Cd Length: 69  Bit Score: 81.70  E-value: 2.56e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958677271  34 RNWCSYvvtRTVSCHVQNGT--YLQRV----LQSCPWPVGCPgnSYRTVVRPMYKVMYKTVTAREWRCCPGHSG 101
Cdd:pfam07546   1 RNVCAY---KVVSCVVVTGTesYVQPVykpyLTWCAGHRRCS--TYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 321-370 1.92e-11

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 59.04  E-value: 1.92e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958677271 321 GHMGTPGPSGPKGTSGPPGEKGERGLPGEPGPQGLMGFPGEPGPKGDPGE 370
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 324-371 3.41e-10

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 55.19  E-value: 3.41e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958677271 324 GTPGPSGPKGTSGPPGEKGERGLPGEPGPQGLMGFPGEPGPKGDPGEK 371
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPP 48
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 321-369 2.33e-07

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 52.60  E-value: 2.33e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958677271 321 GHMGTPGPSGPKGTSGPPGEKGERGLPGEPGPQGLMGFPGEPGPKGDPG 369
Cdd:NF038329  239 GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 297-376 4.23e-07

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 51.83  E-value: 4.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677271 297 GPPGPPGPMGPPGLPGPTGAPGSPGHMGTPGPSGPKGTSGPPGEKGERGLPGEPGPQGLMGFPGEPGPKGDPGEKSHWGE 376
Cdd:NF038329  147 GPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGP 226
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 300-377 6.36e-05

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 44.90  E-value: 6.36e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958677271 300 GPPGPMGPpglpgptgapgsPGHMGTPGPSGPKGTSGPPGEKGERGLPGEPGPQGLMGFPGEPGPKGDPGEKSHWGEG 377
Cdd:NF038329  168 GEAGPQGP------------AGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG 233
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 189-376 5.38e-04

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 42.20  E-value: 5.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677271 189 DGGLQDRVDSWEL--PGPTGPKGDTDRQDPirirgppgpQGPPGRPGQTGAAGTPGKMGPPGPPGPPGPPGPPAPVGPPS 266
Cdd:NF038329  107 DEGLQQLKGDGEKgePGPAGPAGPAGEQGP---------RGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958677271 267 AQvslhGDPLLSNTFTEMGSHWPQGPTGPPGPPGPPGPMGPPGLPGPTGAPGSPGHMG--TPGPSGPKGTSGPPGEKGER 344
Cdd:NF038329  178 KD----GEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPD 253

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958677271 345 GLPGEPGPQGLMGFPGEPGPKGDPGEKSHWGE 376
Cdd:NF038329  254 GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 345-376 2.03e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 36.32  E-value: 2.03e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958677271 345 GLPGEPGPQGLMGFPGEPGPKGDPGEKSHWGE 376
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGE 32
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 305-370 6.88e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 38.73  E-value: 6.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958677271 305 MGPPGLPGPTGAPGSPGHMGTPGPSGPKGTSGPPGEKGERGLPGEPGPQGLMGFPGEPGPKGDPGE 370
Cdd:NF038329  253 DGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK 318
 
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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